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Identification of novel interaction partners for the conserved membrane proximal region of α‐integrin cytoplasmic domains
Author(s) -
Wixler Viktor,
Laplantine Emmanuel,
Geerts Dirk,
Sonnenberg Arnoud,
Petersohn Dirk,
Eckes Beate,
Paulsson Mats,
Aumailley Monique
Publication year - 1999
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(99)00151-9
Subject(s) - integrin, beta 6 , integrin , complementary dna , biology , protein subunit , cytoplasm , integrin alpha m , cd49c , microbiology and biotechnology , cdna library , gene isoform , receptor , gene , genetics
The α3Aβ1 integrin is a laminin receptor with a broad specificity for different laminin isoforms. Furthermore, it regulates the function of other integrins, like α2β1, α5β1 and α6Aβ1. In a yeast two hybrid screen of a human placenta cDNA library, we identified cDNAs coding for four different proteins that strongly interact with the conserved region of the cytoplasmic domain of the α3A integrin subunit. In addition to the cDNA for nucleotide exchange factor Mss4 and the putative tumour suppressor protein BIN1, two novel cDNAs were identified. Association analysis with different integrin subunits revealed them as cDNAs that encode binding proteins which react with a broad spectrum of α subunits. The conserved membrane proximal region of the α3A chain was identified as the binding site for all four proteins. They, therefore, may be involved in the regulation of general functions of integrins.