Multiprotein signalling complexes: regional assembly on heparan sulphate.
Authors
Gallagher, John TAffiliation
CRUK Department of Medical Oncology, University of Manchester, Paterson Institute for Cancer Research, UK. jgallagher@picr.man.ac.ukIssue Date
2006-06
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Heparan sulphate (HS) is an abundant component of cell surfaces and the extracellular matrix. It binds to a wide variety of peptide growth factors, morphogens, chemokines and extracellular matrix proteins (e.g. fibronectin) and many of these interactions are essential for these effector proteins to transduce signals across the plasma membrane. The unique molecular design and flexibility of HS are essential for its ability to exert control over the cellular response to proteinaceous ligands. The clustering of sulphated sugar residues in a series of complex domains with variable sulphation patterns generates considerable diversity in the molecular fine structure of HS. This diversity reflects a high degree of selectivity in protein recognition and in the assembly of functional multiprotein complexes on the HS polymer chain.Citation
Multiprotein signalling complexes: regional assembly on heparan sulphate. 2006, 34 (Pt 3):438-41 Biochem. Soc. Trans.Journal
Biochemical Society TransactionsDOI
10.1042/BST0340438PubMed ID
16709181Type
ArticleLanguage
enISSN
0300-5127ae974a485f413a2113503eed53cd6c53
10.1042/BST0340438
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