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Sökning: id:"swepub:oai:DiVA.org:sh-15811" > Functional interact...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003176naa a2200385 4500
001oai:DiVA.org:sh-15811
003SwePub
008120307s2002 | |||||||||||000 ||eng|
009oai:prod.swepub.kib.ki.se:1933165
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:sh:diva-158112 URI
0247 a https://doi.org/10.1074/jbc.M1085372002 DOI
0247 a http://kipublications.ki.se/Default.aspx?queryparsed=id:19331652 URI
040 a (SwePub)shd (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Vargas, Lu Karolinska Institutet4 aut
2451 0a Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx
264 1c 2002
338 a print2 rdacarrier
520 a Bruton's tyrosine kinase (Btk), a member of the Tec family of protein-tyrosine kinases, has been shown to be crucial for B cell development, differentiation, and signaling. Mutations in the Btk gene lead to X-linked agammaglobulinemia in humans and X-linked immunodeficiency in mice. Using a co-transfection approach, we present evidence here that Btk interacts physically with caveolin-1, a 22-kDa integral membrane protein, which is the principal structural and regulatory component of caveolae membranes. In addition, we found that native Bmx, another member of the Tec family kinases, is associated with endogenous caveolin-1 in primary human umbilical vein endothelial cells. Second, in transient transfection assays, expression of caveolin-1 leads to a substantial reduction in the in vivo tyrosine phosphorylation of both Btk and its constitutively active form, E41K. Furthermore, a caveolin-1 scaffolding peptide (amino acids 82-101) functionally suppressed the autokinase activity of purified recombinant Btk protein. Third, we demonstrate that mouse splenic B-lymphocytes express substantial amounts of caveolin-1. Interestingly, caveolin-1 was found to be constitutively phosphorylated on tyrosine 14 in these cells. The expression of caveolin-1 in B-lymphocytes and its interaction with Btk may have implications not only for B cell activation and signaling, but also for antigen presentation.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
7001 a Nore, B Fu Karolinska Institutet4 aut
7001 a Berglöf, Au Karolinska Institutet4 aut
7001 a Heinonen, J E4 aut
7001 a Mattsson, P T4 aut
7001 a Smith, C I Eu Karolinska Institutet4 aut
7001 a Mohamed, Abdalla Ju Karolinska Institutet,Södertörns högskola,Avdelning Naturvetenskap,Karolinska Institute4 aut0 (Swepub:sh)SHADJA
7102 a Karolinska Institutetb Avdelning Naturvetenskap4 org
7730 t Journal of Biological Chemistryg 277:11, s. 9351-9357q 277:11<9351-9357x 0021-9258x 1083-351X
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:sh:diva-15811
8564 8u https://doi.org/10.1074/jbc.M108537200
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:1933165

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