Abstract:
:The single-pass transmembrane domains (TMDs) of the syndecan family of cell surface adhesion molecules have been implicated in functional protein-protein interactions. Although each paralog contains a conserved GxxxG dimerization motif, we show here that the syndecan-1 TMD dimerizes weakly, the syndecan-3 and syndecan-4 TMDs each dimerize strongly, and the syndecan-2 TMD dimerizes very strongly. These markedly different levels of self-association suggest that paralog TMDs play different roles in directing functional interactions of each full-length syndecan family member. We further show that each syndecan TMD forms detergent-resistant heteromeric complexes with other paralogs, and that these interactions exhibit selectivity. Although heteromeric interactions among full-length syndecan paralogs have not been reported, we argue that the distinct hierarchy of protein-protein interactions mediated by the syndecan TMDs may give rise to considerable complexity in syndecan function. The demonstration that TMD homodimerization and heterodimerization can be mediated by GxxxG motifs and modulated by sequence context has implications for the signaling mechanisms of other cell surface receptors, including the integrins and the erbB family.
journal_name
Proc Natl Acad Sci U S Aauthors
Dews IC,Mackenzie KRdoi
10.1073/pnas.0708909105subject
Has Abstractpub_date
2007-12-26 00:00:00pages
20782-7issue
52eissn
0027-8424issn
1091-6490pii
0708909105journal_volume
104pub_type
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