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The integrin α V β 6 binds and activates latent TGFβ3
Author(s) -
Annes Justin P.,
Rifkin Daniel B.,
Munger John S.
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03280-x
Subject(s) - transforming growth factor , gene isoform , transforming growth factor beta , chemistry , microbiology and biotechnology , protein precursor , integrin , peptide , receptor , biology , biochemistry , gene
Transforming growth factors‐β (TGFβ1, 2 and 3) are secreted in a complex with their propeptides (latency‐associated peptide 1 (LAP1), 2 and 3). TGFβ signaling requires the dissociation of LAP and TGFβ, a process termed latent TGFβ activation. This process is a critical but incompletely understood step in the regulation of TGFβ function. In particular, the extent to which activation mechanisms differ among the three TGFβ isoforms is relatively unexplored. We show here that α V β 6 binds and activates latent TGFβ3.