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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_sdt=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: [email protected] .

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

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”

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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 …

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 753 Related articles All 10 versions Cite Saved

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 851 Related articles All 9 versions Cite Saved More

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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 267 Related articles All 6 versions Cite Saved More

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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 473 Related articles All 7 versions Cite Saved More

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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

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 127 Related articles All 6 versions Cite Saved More

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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 107 Related articles All 4 versions Cite Saved More

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 77 Related articles All 5 versions Cite Saved More

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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 356 Related articles All 4 versions Cite Saved More

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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 239 Related articles All 5 versions Cite SaveSaved More

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[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 1543 Related articles All 9 versions Cite SaveSaved More

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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 62 Related articles All 4 versions Cite Saved

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 270 Related articles All 7 versions Cite SaveSaved 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 ...


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Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin FUNCTIONAL SIGNIFICANCE OF THE NOS CAVEOLIN BINDING DOMAININ VIVO

G Garcıa-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 741 Related articles All 6 versions Cite Saved More

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[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 ...


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… 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 ...


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[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


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[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

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 ...


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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 ...


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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 ...


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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 ...

Cited by 21 Related articles All 7 versions Cite SaveSaved

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