Change search
Link to record
Permanent link

Direct link
Mohamed, Abdalla J
Publications (2 of 2) Show all publications
Arteaga, H. J., Hinkula, J., van Dijk-Hard, I., Dilber, M. S., Wahren, B., Christensson, B., . . . Smith, C. I. (2003). Choosing CCR5 or Rev siRNA in HIV-1. Nature Biotechnology, 21(3), 230-231
Open this publication in new window or tab >>Choosing CCR5 or Rev siRNA in HIV-1
Show others...
2003 (English)In: Nature Biotechnology, ISSN 1087-0156, E-ISSN 1546-1696, Vol. 21, no 3, p. 230-231Article in journal (Refereed) Published
National Category
Biological Sciences
urn:nbn:se:sh:diva-15636 (URN)10.1038/nbt0303-230 (DOI)000181312500013 ()
Available from: 2012-02-23 Created: 2012-02-22 Last updated: 2017-12-07Bibliographically approved
Vargas, L., Nore, B. F., Berglöf, A., Heinonen, J. E., Mattsson, P. T., Smith, C. I. & Mohamed, A. J. (2002). Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx. Journal of Biological Chemistry, 277(11), 9351-9357
Open this publication in new window or tab >>Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx
Show others...
2002 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 277, no 11, p. 9351-9357Article in journal (Refereed) Published
Abstract [en]

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.

National Category
Biochemistry and Molecular Biology
urn:nbn:se:sh:diva-15811 (URN)10.1074/jbc.M108537200 (DOI)000174400600083 ()11751885 (PubMedID)2-s2.0-0037088646 (Scopus ID)
Available from: 2012-03-08 Created: 2012-03-07 Last updated: 2017-12-07Bibliographically approved

Search in DiVA

Show all publications