Skp2 induction and phosphorylation is associated with the late G1 phase of proliferating rat hepatocytes.

Abstract:

:The changes in phosphoproteins purified with the affinity peptide p9CKShs1 were analyzed from extracts of regenerating rat livers in order to define some G1 and G1/S regulations characteristic of mature hepatocytes stimulated to proliferate. We observed a 47 kDa phosphoprotein that occurred first at the end of G1 before peaking in the S phase. P47 was also found to be phosphorylated in late G1 in primary hepatocyte cultures stimulated with mitogens. P47 was still phosphorylated in extracts depleted of Cdc2, but to a lesser extent after Cdk2 depletion. This phosphoprotein was identified as Skp2. (i) P47 shared the same electrophoretic mobility than Skp2, a cell cycle protein essential for S phase entry in human fibroblasts; (ii) Skp2, like P47, started to be expressed and was highly phosphorylated during the G1/S transition of hepatocytes stimulated to proliferate in vivo and in vitro; (iii) P47 was specifically immunoprecipitated by an antibody directed against Skp2. In addition, cyclin A/Cdk2 complexes from regenerating liver clearly interacted with Skp2. This is the first demonstration that Skp2 is induced and phosphorylated in the late G1 and S phase of hepatocytes in vivo in regenerating liver as well as in vitro in mitogen-stimulated hepatocytes.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Bilodeau M,Talarmin H,Ilyin G,Rescan C,Glaise D,Cariou S,Loyer P,Guguen-Guillouzo C,Baffet G

doi

10.1016/s0014-5793(99)00629-8

keywords:

subject

Has Abstract

pub_date

1999-06-11 00:00:00

pages

247-53

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(99)00629-8

journal_volume

452

pub_type

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