- The caveolin scaffolding domain was first identified and termed in 1996. It is a 20 amino acid region within caveolin that interacts with signaling proteins like Src kinases.
- The caveolin scaffolding domain negatively regulates the activity of Src kinases and other signaling molecules by preferentially interacting with their inactive conformations.
- This scaffolding domain is important for caveolin oligomerization and organization of "pre-assembled signaling complexes" within caveolae membrane domains.
Kupffer Cells Mediate Leptin-Induced Liver Fibrosis.
GASTROENTEROLOGY 2009;137:713–723
JIANHUA WANG,* ISABELLE LECLERCQ,‡ JOANNE M. BRYMORA,* NING XU,* MEHDI RAMEZANI–MOGHADAM,* ROSLYN M. LONDON,* DAVID BRIGSTOCK,§ and JACOB GEORGE*
*Storr Liver Unit, Westmead Millennium Institute, University of Sydney and Westmead Hospital, Westmead, Australia; ‡Laboratory of Gastroenterology, Faculty of
Medicine, Université Catholique de Louvain, Brussels, Belgium; and §Center for Cell and Vascular Biology, Children’s Research Institute, Columbus, Ohio
瘦素(Leptin)是一由脂肪細胞(Adipocyte)所分泌之荷爾蒙,是調控體重及新陳代謝之重要因子。過去研究發現病態肥胖(Obese)、脂肪肝(Nonalcoholic steatohepatitis)及酒精性肝炎(Alcoholic liver disease)等病患之血液循環中,Leptin量有明顯增加。而近期研究報告指出leptin具有促進肝臟纖維化(Liver fibrosis)之能力,當中分子機理並未明確。
在肝纖維化過程中,肝臟星狀細胞(HSC)會被活化增生及促進胞外基質(ECM)產生,而鄰近之Kupffer細胞(KC)則已知可透過促發炎因子(Proinflammatory factor)和促纖維化因子(Profibrogenic factors)例如TGF-β1和ROS影響HSC表現。雖然HSC是肝纖維化過程中重要角色,前人研究卻發現leptin似對HSC無任何調控作用。故本篇作者針對Leptin是否透過間接作用於HSC鄰近之KC,刺激其產生促纖維化因子,以活化HSC。
為探討leptin直接或間接影響HSC之分子機理,本篇作者透過RT-PCR、Immunoblot等分子生物學方法,分別測定leptin刺激後HSC及KC中Collagen I、TIMP1等促纖維化因子基因及蛋白表現,發現leptin雖可促使HSC增生,但對其纖維化能力之影響甚微。而leptin可刺激KC中TGF-β1及CTGF/CCN2等肝纖維化中重要之cytokines表現。另發現Leptin-treated KC-conditioned培養液可刺激HSC增生及增加其中Collagen I、TIMP1等表現,得出了leptin是透過刺激KC來活化HSC之推論。作者亦於後續實驗中,透過磷酸化測定、EMSA等方法探討leptin訊號傳遞作用,發現leptin可活化KC中STAT3、ERK1/2、AKT等路徑,及下游因子AP-1、NF-κB,而此兩種蛋白具有增強TGF-β1及CTGF/CCN2基因表現之能力。
Kupffer Cells Mediate Leptin-Induced Liver Fibrosis.
GASTROENTEROLOGY 2009;137:713–723
JIANHUA WANG,* ISABELLE LECLERCQ,‡ JOANNE M. BRYMORA,* NING XU,* MEHDI RAMEZANI–MOGHADAM,* ROSLYN M. LONDON,* DAVID BRIGSTOCK,§ and JACOB GEORGE*
*Storr Liver Unit, Westmead Millennium Institute, University of Sydney and Westmead Hospital, Westmead, Australia; ‡Laboratory of Gastroenterology, Faculty of
Medicine, Université Catholique de Louvain, Brussels, Belgium; and §Center for Cell and Vascular Biology, Children’s Research Institute, Columbus, Ohio
瘦素(Leptin)是一由脂肪細胞(Adipocyte)所分泌之荷爾蒙,是調控體重及新陳代謝之重要因子。過去研究發現病態肥胖(Obese)、脂肪肝(Nonalcoholic steatohepatitis)及酒精性肝炎(Alcoholic liver disease)等病患之血液循環中,Leptin量有明顯增加。而近期研究報告指出leptin具有促進肝臟纖維化(Liver fibrosis)之能力,當中分子機理並未明確。
在肝纖維化過程中,肝臟星狀細胞(HSC)會被活化增生及促進胞外基質(ECM)產生,而鄰近之Kupffer細胞(KC)則已知可透過促發炎因子(Proinflammatory factor)和促纖維化因子(Profibrogenic factors)例如TGF-β1和ROS影響HSC表現。雖然HSC是肝纖維化過程中重要角色,前人研究卻發現leptin似對HSC無任何調控作用。故本篇作者針對Leptin是否透過間接作用於HSC鄰近之KC,刺激其產生促纖維化因子,以活化HSC。
為探討leptin直接或間接影響HSC之分子機理,本篇作者透過RT-PCR、Immunoblot等分子生物學方法,分別測定leptin刺激後HSC及KC中Collagen I、TIMP1等促纖維化因子基因及蛋白表現,發現leptin雖可促使HSC增生,但對其纖維化能力之影響甚微。而leptin可刺激KC中TGF-β1及CTGF/CCN2等肝纖維化中重要之cytokines表現。另發現Leptin-treated KC-conditioned培養液可刺激HSC增生及增加其中Collagen I、TIMP1等表現,得出了leptin是透過刺激KC來活化HSC之推論。作者亦於後續實驗中,透過磷酸化測定、EMSA等方法探討leptin訊號傳遞作用,發現leptin可活化KC中STAT3、ERK1/2、AKT等路徑,及下游因子AP-1、NF-κB,而此兩種蛋白具有增強TGF-β1及CTGF/CCN2基因表現之能力。
Continuing with the theme of DNA repair via homologous recombination, I will discuss the following family during the PAINT call:
PTHR13451 CLASS II CROSSOVER JUNCTION ENDONUCLEASE MUS81
The Beta Amyloid Cleaving Enzymes: From Drug Discovery to Evolution and BackChris Southan
Slides presented at the University of Edinburgh in Jan 2014, based on our paper "A tale of two drug targets: the evolutionary history of BACE1 and BACE2" http://www.ncbi.nlm.nih.gov/pubmed/24381583
The beta amyloid (APP) cleaving enzyme (BACE1) has been a drug target for Alzheimer's Disease (AD) since 1999 with lead inhibitors now entering clinical trials. In 2011, the paralog, BACE2, became a new target for type II diabetes (T2DM) having been identified as a TMEM27 secretase regulating pancreatic β cell function. However, the normal roles of both enzymes are unclear. This study outlines their evolutionary history and new opportunities for functional genomics. We identified 30 homologs (UrBACEs) in basal phyla including Placozoans, Cnidarians, Choanoflagellates, Porifera, Echinoderms, Annelids, Mollusks and Ascidians (but not Ecdysozoans). UrBACEs are predominantly single copy, show 35–45% protein sequence identity with mammalian BACE1, are ~100 residues longer than cathepsin paralogs with an aspartyl protease domain flanked by a signal peptide and a C-terminal transmembrane domain. While multiple paralogs in Trichoplax and Monosiga pre-date the nervous system, duplication of the UrBACE in fish gave rise to BACE1 and BACE2 in the vertebrate lineage. The latter evolved more rapidly as the former maintained the emergent neuronal role. In mammals, Ka/Ks for BACE2 is higher than BACE1 but low ratios for both suggest purifying selection. The 5' exons show higher Ka/Ks than the catalytic section. Model organism genomes show the absence of certain BACE human substrates when the UrBACE is present. Experiments could thus reveal undiscovered substrates and roles. The human protease double-target status means that evolutionary trajectories and functional shifts associated with different substrates will have implications for the development of clinical candidates for both AD and T2DM. A rational basis for inhibition specificity ratios and assessing target-related side effects will be facilitated by a more complete picture of BACE1 and BACE2 functions informed by their evolutionary context.
Chaperones are a functionally related group of proteins that assist the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures.
HIGHER EDUCATION POWERED BY TECHNOLOGY
A powerful instrument for change
The following slides have been created by Intel for public use. Share or use the presentation in its entirety or as individual slides as desired.
Continuing with the theme of DNA repair via homologous recombination, I will discuss the following family during the PAINT call:
PTHR13451 CLASS II CROSSOVER JUNCTION ENDONUCLEASE MUS81
The Beta Amyloid Cleaving Enzymes: From Drug Discovery to Evolution and BackChris Southan
Slides presented at the University of Edinburgh in Jan 2014, based on our paper "A tale of two drug targets: the evolutionary history of BACE1 and BACE2" http://www.ncbi.nlm.nih.gov/pubmed/24381583
The beta amyloid (APP) cleaving enzyme (BACE1) has been a drug target for Alzheimer's Disease (AD) since 1999 with lead inhibitors now entering clinical trials. In 2011, the paralog, BACE2, became a new target for type II diabetes (T2DM) having been identified as a TMEM27 secretase regulating pancreatic β cell function. However, the normal roles of both enzymes are unclear. This study outlines their evolutionary history and new opportunities for functional genomics. We identified 30 homologs (UrBACEs) in basal phyla including Placozoans, Cnidarians, Choanoflagellates, Porifera, Echinoderms, Annelids, Mollusks and Ascidians (but not Ecdysozoans). UrBACEs are predominantly single copy, show 35–45% protein sequence identity with mammalian BACE1, are ~100 residues longer than cathepsin paralogs with an aspartyl protease domain flanked by a signal peptide and a C-terminal transmembrane domain. While multiple paralogs in Trichoplax and Monosiga pre-date the nervous system, duplication of the UrBACE in fish gave rise to BACE1 and BACE2 in the vertebrate lineage. The latter evolved more rapidly as the former maintained the emergent neuronal role. In mammals, Ka/Ks for BACE2 is higher than BACE1 but low ratios for both suggest purifying selection. The 5' exons show higher Ka/Ks than the catalytic section. Model organism genomes show the absence of certain BACE human substrates when the UrBACE is present. Experiments could thus reveal undiscovered substrates and roles. The human protease double-target status means that evolutionary trajectories and functional shifts associated with different substrates will have implications for the development of clinical candidates for both AD and T2DM. A rational basis for inhibition specificity ratios and assessing target-related side effects will be facilitated by a more complete picture of BACE1 and BACE2 functions informed by their evolutionary context.
Chaperones are a functionally related group of proteins that assist the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures.
HIGHER EDUCATION POWERED BY TECHNOLOGY
A powerful instrument for change
The following slides have been created by Intel for public use. Share or use the presentation in its entirety or as individual slides as desired.
Crisi= A time of danger "OR" A Time of opportunityDavide Geraci
Ampliare o migliorare il proprio modello di acquisizione.
Ha Realizzato per le Aziende Italiane di eccellenza un polo dedicato al “Made in Italy”.
Ha una estensione totale di 454.000 mq, ed è composto da un area Espositiva di oltre 87.000 mq, che vedrà l’apertura di spazi commerciali permanenti per la vendita di Beni e Servizi.
Il polo mira ad attirare i consumatori Privati, ma soprattutto Buyer, Distributori e Importatori Cinesi.
Il governo Nazionale di Pechino in collaborazione con la Municipalità di HANGZHOU, ed in partenariato con “Confimprese/NordOvest”, si occuperà dell’attuazione del progetto.
Los profesores Jonathan P. Wojciechowski y Molly M. Stevens, nota realizada en la revista Science, con motivo del artículo publicado por Ivan Sasselli. Revista Science, 374 (6569), • DOI: 10.1126/science.abh3602
Applications of protein array in diagnostics and genomic and proteomicSusan Rey
icroarray technology can simultaneously analyze thousands of parameters in a single experiment. Micro-point of capture molecules are fixed into ranks on a solid support and exposed to samples containing corresponding binding molecules. Complex formation in each micro-point can be detected by the readout system, which is based on fluorescence, chemiluminescence, mass spectrometry, radioactive or electrochemistry. Miniaturization and parallelization binding assays, whose analysis power can be also enlarged by microarray gene expression analysis, is sensitive. These systems can be used to detect the degree of hybridization and immobilized DNA microarray probes will be exposed to complementary target. Currently, the development of protein array has demonstrated its applications in enzyme-substrate, DNA- protein and different types of protein - protein interactions. In this post, we will discuss the capture-molecule-ligand analysis, analyze its theoretical advantages and disadvantage and its influence in diagnostics, genomic and proteomics.
Applications of protein array in diagnostics and genomic and proteomicSusan Rey
Microarray technology can simultaneously analyze thousands of parameters in a single experiment. Micro-point of capture molecules are fixed into ranks on a solid support and exposed to samples containing corresponding binding molecules. Complex formation in each micro-point can be detected by the readout system, which is based on fluorescence, chemiluminescence, mass spectrometry, radioactive or electrochemistry. Miniaturization and parallelization binding assays, whose analysis power can be also enlarged by microarray gene expression analysis, is sensitive. These systems can be used to detect the degree of hybridization and immobilized DNA microarray probes will be exposed to complementary target. Currently, the development of protein array has demonstrated its applications in enzyme-substrate, DNA- protein and different types of protein - protein interactions. In this post, we will discuss the capture-molecule-ligand analysis, analyze its theoretical advantages and disadvantage and its influence in diagnostics, genomic and proteomics.
Oncology: Spatial Localization of Ras proteinsNachiket Vartak
This is a presentation of work done at the MPI Dortmund from 2008-2013 on the mechanism through with localization of the Ras protein in generated in cells. It presents the inhibiton Palmostatin-B, which inhibits this mechanism, leading to reveral of oncogenic signaling and cancerous phenotypes.
Similar to Google Scholar CSD-cited 17700_PM4840_ v3 (18)
1. Caveolin scaffolding domain
Google Scholar: à 17,700 results (Citations)
PubMed search for “caveolin scaffolding domain” à 4840 citations.
http://scholar.google.com/scholar?hl=en&q=caveolin+scaffolding+domain&btnG=&as_s
dt=1%2C5&as_sdtp=
First time, we termed “caveolin scaffolding domain” – in 1996.
Src Tyrosine Kinases, Gα Subunits, and H-Ras Share a
Common Membrane-anchored Scaffolding Protein,
Caveolin
CAVEOLIN BINDING NEGATIVELY REGULATES THE AUTO-
ACTIVATION OF Src TYROSINE KINASES*
1. Shengwen Li‡,
2. Jacques Couet§ and
3. Michael P. Lisanti¶
+ Author Affiliations
1. From the Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142-1479
1. ¶To whom correspondence should be addressed. Tel.: 617-258-5225; Fax: 617-258-9872; E-mail:
lisanti@wi.mit.edu .
Abstract
Caveolae are plasma membrane specializations present in most cell types. Caveolin, a 22-kDa
integral membrane protein, is a principal structural and regulatory component of caveolae
membranes. Previous studies have demonstrated that caveolin co-purifies with lipid modified
signaling molecules, including Gα subunits, H-Ras, c-Src, and other related Src family tyrosine
kinases. In addition, it has been shown that caveolin interacts directly with Gα subunits and H-Ras,
preferentially recognizing the inactive conformation of these molecules. However, it is not known
whether caveolin interacts directly or indirectly with Src family tyrosine kinases. Here, we examine
the structural and functional interaction of caveolin with Src family tyrosine kinases. Caveolin was
2. recombinantly expressed as a glutathione S-transferase fusion. Using an established in vitro binding
assay, we find that caveolin interacts with wild-type Src (c-Src) but does not form a stable complex
with mutationally activated Src (v-Src). Thus, it appears that caveolin prefers the inactive
conformation of Src. Deletion mutagenesis indicates that the Src-interacting domain of caveolin is
located within residues 82-101, a cytosolic membrane-proximal region of caveolin. A caveolin
peptide derived from this region (residues 82-101) functionally suppressed the auto-activation of
purified recombinant c-Src tyrosine kinase and Fyn, a related Src family tyrosine kinase. We further
analyzed the effect of caveolin on c-Src activity in vivo by transiently co-expressing full-length
caveolin and c-Src tyrosine kinase in 293T cells. Co-expression with caveolin dramatically
suppressed the tyrosine kinase activity of c-Src as measured via an immune complex kinase assay.
Thus, it appears that caveolin structurally and functionally interacts with wild-type c-Src via caveolin
residues 82-101. Besides interacting with Src family kinases, this cytosolic caveolin domain (residues
82-101) has the following unique features. First, it is required to form multivalent homo-oligomers
of caveolin. Second, it interacts with G-protein α-subunits and down-regulates their GTPase activity.
Third, it binds to wild-type H-Ras. Fourth, it is membrane-proximal, suggesting that it may be
involved in other potential protein-protein interactions. Thus, we have termed this 20-amino
acid stretch of caveolin residues the caveolin scaffolding domain.
Reference:
doi: 10.1074/jbc.271.46.29182 November 15, 1996 The Journal of Biological
Chemistry 271, 29182-29190.
http://www.jbc.org/content/271/46/29182.short
PubMed search: Search results for “caveolin scaffolding domain”
Items: 1 to 20 of 244 pages
20 articles per page:
244*20 = 4840 articles cited
http://www.ncbi.nlm.nih.gov/pubmed/?term=caveolin+scaffolding+domain
~~~~
Tyrosine Kinases, Gα Subunits, and H-Ras Share a Common Membrane-
anchored Scaffolding Protein, Caveolin CAVEOLIN BINDING NEGATIVELY
REGULATES …
3. S Li, J Couet, MP Lisanti - Journal of Biological Chemistry, 1996 - ASBMB
... In this regard, several independent lines of evidence suggest that caveolin may function as a
scaffolding protein within caveolae ... Subsequently, these individual caveolin homo-oligomers
(4-6-nm particles) can interact with each other to form caveolae-like structures in vitro ...
Cited by 753Related articlesAll 10 versionsCiteSaved
Identification of peptide and protein ligands for the caveolin-scaffolding domain
Implications for the interaction of caveolin with caveolae-associated proteins
J Couet, S Li, T Okamoto, T Ikezu, MP Lisanti - Journal of Biological …, 1997 - ASBMB
Abstract Caveolin, a 21-24-kDa integral membrane protein, is a principal component of
caveolae membranes. We have suggested that caveolin functions as a scaffolding protein to
organize and concentrate certain caveolin-interacting proteins within caveolae ...
Cited by 851Related articlesAll 9 versionsCiteSavedMore
[HTML] from jbc.org
Caveolin interaction with protein kinase c isoenzyme-dependent regulation of
kinase activity by the caveolin scaffolding domain peptide
N Oka, M Yamamoto, C Schwencke, J Kawabe… - Journal of Biological …, 1997 - ASBMB
Abstract Caveolar localization of protein kinase C and the regulation of caveolar function by
protein kinase C are well known. This study was undertaken to examine whether caveolin
subtypes interact with various protein kinase C isoenzymes using the caveolin scaffolding ...
Cited by 267Related articlesAll 6 versionsCiteSavedMore
[PDF] from researchgate.net
In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide
synthesis and reduces inflammation
M Bucci, JP Gratton, RD Rudic, L Acevedo… - Nature medicine, 2000 - nature.com
Caveolin-1, the primary coat protein of caveolae, has been implicated as a regulator of
signal transduction through binding of its" scaffolding domain" to key signaling molecules.
However, the physiological importance of caveolin-1 in regulating signaling has been ...
Cited by 473Related articlesAll 7 versionsCiteSavedMore
[HTML] from jbc.org
A role for the caveolin scaffolding domain in mediating the membrane
attachment of caveolin-1 The caveolin scaffolding domain is both necessary
and sufficient for …
A Schlegel, RB Schwab, PE Scherer… - Journal of Biological …, 1999 - ASBMB
4. Abstract Here, we have created a series of caveolin-1 (Cav-1) deletion mutants to examine
whether the membrane spanning segment is required for membrane attachment of caveolin-
1 in vivo. One mutant, Cav-1-(1–101), contains only the cytoplasmic N-terminal domain ...
Cited by 127Related articlesAll 6 versionsCiteSavedMore
[PDF] from nih.gov
A neutral sphingomyelinase resides in sphingolipid-enriched microdomains and
is inhibited by the caveolin-scaffolding domain: potential implications in tumour
…
RJ VELDMAN, N MAESTRE, OM ADUIB… - Biochemical …, 2001 - biochemj.org
Abstract Sphingomyelinases hydrolyse sphingomyelin to ceramide, a process involved in
signal-transduction routes leading to apoptosis and various other cellular responses. In the
present study, we investigated the sphingomyelinase content of caveolae, invaginated ...
Cited by 107Related articlesAll 4 versionsCiteSavedMore
Inhibition of PKCα and rhoA translocation in differentiated smooth muscle by a
caveolin scaffolding domain peptide
MJ Taggart, P Leavis, O Feron, KG Morgan - Experimental cell research, 2000 - Elsevier
Receptor-coupled contraction of smooth muscle involves recruitment to the plasma
membrane of downstream effector molecules PKCα and rhoA but the mechanism of this
signal integration is unclear. Caveolins, the principal structural proteins of caveolar ...
Cited by 77Related articlesAll 5 versionsCiteSavedMore
[HTML] from jbc.org
Assembly of Trp1 in a signaling complex associated with caveolin-scaffolding
lipid raft domains
TP Lockwich, X Liu, BB Singh, J Jadlowiec… - Journal of Biological …, 2000 - ASBMB
Abstract Trp1 has been proposed as a component of the store-operated Ca 2+ entry (SOC)
channel. However, neither the molecular mechanism of SOC nor the role of Trp in this
process is yet understood. We have examined possible molecular interactions involved in ...
Cited by 356Related articlesAll 4 versionsCiteSavedMore
[HTML] from jbc.org
Interaction of neuronal nitric-oxide synthase with caveolin-3 in skeletal muscle
Identification of a novel caveolin scaffolding/inhibitory domain
VJ Venema, H Ju, R Zou, RC Venema - Journal of Biological Chemistry, 1997 - ASBMB
Abstract Neuronal nitric-oxide synthase (nNOS) has been shown previously to interact with α
1-syntrophin in the dystrophin complex of skeletal muscle. In the present study, we have
examined whether nNOS also interacts with caveolin-3 in skeletal muscle. nNOS and ...
Cited by 239Related articlesAll 5 versionsCiteSaveSaved More
[HTML] from jbc.org
5. [HTML] Caveolins, a family of scaffolding proteins for organizing “preassembled
signaling complexes” at the plasma membrane
T Okamoto, A Schlegel, PE Scherer… - Journal of Biological …, 1998 - ASBMB
... oligomers to interact with each other, thereby forming a caveolin-rich scaffold (14). ... and inactivation
of a diverse group of signaling molecules within caveolae membranes for ... Thus, the caveolin
scaffolding domain may function like other modular protein domains (Src homology-2 ...
Cited by 1543Related articlesAll 9 versionsCiteSaveSaved More
[HTML] from jbc.org
The caveolin scaffolding domain modifies 2-amino-3-hydroxy-5-methyl-4-
isoxazole propionate receptor binding properties by inhibiting phospholipase A2
activity
SB Gaudreault, C Chabot, JP Gratton… - Journal of Biological …, 2004 - ASBMB
Abstract Activation of the enzyme phospholipase (PLA 2) has been proposed to be part of
the molecular mechanism involved in the alteration of 2-amino-3-hydroxy-5-methyl-4-
isoxazole propionate (AMPA) glutamate receptor responsiveness during long term ...
Cited by 62Related articlesAll 4 versionsCiteSaved
Caveolin-1 maintains activated Akt in prostate cancer cells through scaffolding
domain binding site interactions with and inhibition of serine/threonine protein …
L Li, CH Ren, SA Tahir, C Ren… - Molecular and cellular …, 2003 - Am Soc Microbiol
ABSTRACT Previously it has been reported that caveolin-1 (cav-1) has antiapoptotic
activities in prostate cancer cells and functions downstream of androgenic stimulation. In this
study, we demonstrate that cav-1 overexpression significantly reduced thapsigargin (Tg)- ...
Cited by 270Related articlesAll 7 versionsCiteSaveSaved More
[PDF] from donarmstrong.com
Caveolin scaffolding region and cholesterol-rich domains in membranes
RM Epand, BG Sayer, RF Epand - Journal of molecular biology, 2005 - Elsevier
A protein that constitutes a good marker for a type of cholesterol-rich domain in biological
membranes is caveolin. A segment of this protein has a sequence that corresponds to a
cholesterol recognition/interaction amino acid consensus (CRAC) motif; this motif has ...
Cited by 94Related articlesAll 9 versionsCiteSaveSaved More
[HTML] from jbc.org
Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin
FUNCTIONAL SIGNIFICANCE OF THE NOS CAVEOLIN BINDING DOMAININ
VIVO
6. G Garcı́a-Cardeña, P Martasek, BSS Masters… - Journal of Biological …, 1997 - ASBMB
... with both caveolin-1 and caveolin-3 and nNOS localizes in plasmalemmal domains of skeletal
muscle by virtue of its binding to dystrophin complexes (20), which are enriched in
caveolin-3-coated caveolae (21), we tested the ability of the scaffolding domain peptides derived ...
Cited by 741Related articlesAll 6 versionsCiteSavedMore
[HTML] from plos.org
[HTML] Evaluating caveolin interactions: do proteins interact with the caveolin
scaffolding domain through a widespread aromatic residue-rich motif?
DP Byrne, C Dart, DJ Rigden - PloS one, 2012 - journals.plos.org
Abstract Caveolins are coat proteins of caveolae, small flask-shaped pits of the plasma
membranes of most cells. Aside from roles in caveolae formation, caveolins recruit, retain
and regulate many caveolae-associated signalling molecules. Caveolin-protein ...
Cited by 35Related articlesAll 11 versionsCiteSaveSaved More
[HTML] from jbc.org
… Tyrosine Kinases, Gα Subunits, and H-Ras Share a Common Membrane-
anchored Scaffolding Protein, Caveolin CAVEOLIN BINDING NEGATIVELY
REGULATES …
S Li, J Couet, MP Lisanti - Journal of Biological Chemistry, 1996 - ASBMB
... In this regard, several independent lines of evidence suggest that caveolin may function as a
scaffolding protein within caveolae ... Subsequently, these individual caveolin homo-oligomers
(4-6-nm particles) can interact with each other to form caveolae-like structures in vitro ...
Cited by 753Related articlesAll 10 versionsCiteSavedMore
Free from Publisher
[CITATION] Caveolin-1 regulates store-operated Ca2+ influx by binding of its
scaffolding domain to transient receptor potential channel-1 in endothelial cells
AM Kwiatek, RD Minshall, DR Cool, RA Skidgel… - Molecular …, 2006 - ASPET
Cited by 86Related articlesAll 6 versionsCiteSavedMore
[HTML] from physiology.org
[HTML] Antifibrotic properties of caveolin-1 scaffolding domain in vitro and in vivo
E Tourkina, M Richard, P Gööz… - American Journal of …, 2008 - Am Physiological Soc
7. Abstract Lung fibrosis involves the overexpression of ECM proteins, primarily collagen, by α-
smooth muscle actin (ASMA)-positive cells. Caveolin-1 is a master regulator of collagen
expression by cultured lung fibroblasts and of lung fibrosis in vivo. A peptide equivalent to ...
Cited by 94Related articlesAll 6 versionsCiteSaveSaved More
[HTML] from jbc.org
Caveolin versus calmodulin counterbalancing allosteric modulators of
endothelial nitric oxide synthase
JB Michel, O Feron, K Sase, P Prabhakar… - Journal of Biological …, 1997 - ASBMB
... an oligomeric integral membrane protein that appears to serve as the structural “scaffold” within
caveolae. ... 7, 24) has led to the discovery of a direct interaction between caveolin and such ... α s .
These interactions appear to be mediated through a scaffolding domain comprising a ...
Cited by 342Related articlesAll 8 versionsCiteSaveSaved More
[HTML] from jbc.org
Interaction of a receptor tyrosine kinase, EGF-R, with caveolins Caveolin binding
negatively regulates tyrosine and serine/threonine kinase activities
J Couet, M Sargiacomo, MP Lisanti - Journal of Biological Chemistry, 1997 - ASBMB
... direct interaction of caveolin with a growth factor receptor, EGF-R, a known caveolae-associated
receptor ... We now show that this caveolin binding motif within the kinase domain of the EGF-R
can mediate the interaction of the EGF-R with the scaffolding domains of caveolins ...
Cited by 589Related articlesAll 6 versionsCiteSaveSaved More
[HTML] from wiley.com
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[HTML] Role of the membrane interface on the conformation of the caveolin
scaffolding domain: a CD and NMR study
CL Lan, JM Neumann, N Jamin - FEBS letters, 2006 - Wiley Online Library
Abstract Circular dichroism (CD) and NMR spectroscopy were used to study the
conformational properties of two synthetic peptides, D82–R101 and D82–I109,
encompassing the caveolin scaffolding domain (D82–R101), in the presence of ...
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