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Regulation of multiple functions of SHPS-1, a transmembrane glycoprotein, by its cytoplasmic region.

Abstract：

:SHPS-1 is a receptor-type transmembrane glycoprotein, which contains four tyrosine residues in its cytoplasmic region, and the phosphorylation of these tyrosine residues serves the binding sites for SHP-2 protein-tyrosine phosphatase. Its extracellular region interacts with another membrane protein, CD47, thereby constituting a cell-cell communication system. We analyzed this ligand-receptor interaction using Chinese hamster ovary (CHO) cells expressing wild-type (WT) or mutant SHPS-1. The binding affinity of an SHPS-1 mutant such as deltaCyto, that lacked most of cytoplasmic region, or 4F, in which all four tyrosine residues in cytoplasmic region were substituted with phenylalanine, for a recombinant CD47-Fc was greater than that of WT. In addition, oligomerization of deltaCyto or 4F mutant by binding of CD47-Fc was greater than WT. Chemical cross-linking of SHPS-1 indicated that SHPS-1 formed a cis-dimer. Furthermore, WT cells exhibited a less polarized cell shape with decreased formation of actin stress fibers, compared with parental CHO cells and mutant SHPS-1 expressing cells. Prominent lamellipodium formation and membrane ruffling were also observed at leading edges of migrating WT cells but not at those of other mutant SHPS-1 expressing cells. These results suggest that the binding affinity of SHPS-1 to CD47, clustering ability of SHPS-1, and cytoskeletal reorganization are regulated by the cytoplasmic region of SHPS-1.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Sato R,Ohnishi H,Kobayashi H,Kiuchi D,Hayashi A,Kaneko Y,Honma N,Okazawa H,Hirata Y,Matozaki T

doi

10.1016/j.bbrc.2003.08.031

subject

Has Abstract

pub_date

2003-09-26 00:00:00

pages

584-90

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X03016164

journal_volume

309

pub_type

杂志文章

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