Identification and properties of an atypical catalytic subunit (p34PSK-J3/cdk4) for mammalian D type G1 cyclins

H Matsushime, ME Ewen, DK Strom, JY Kato… - Cell, 1992 - cell.com
H Matsushime, ME Ewen, DK Strom, JY Kato, SK Hanks, MF Roussel, CJ Sherr
Cell, 1992cell.com
Murine Dtypecyclinsassociate with a catalytic subunit (p34PSK. J7 with properties distinct
from known cyclindependent kinases (cdks). Mouse p34psK. J3 shows less than 50% amino
acid identity to p34-,~ 33~*~~, and p360dk3, lacks a PSTAIRE motif, and does not bind to
p13* Uc'. Cyclin Dl-p34psK. J3 complexes accumulate in macrophages during Gl and
decline in S phase, whereas complexes involving cyclins D2 and D3 form in proliferating T
cells. Although histone Hl kinase activity is not detected in cyclin D or PSK-J3 …
Summary
Murine Dtypecyclinsassociate with a catalytic subunit (p34PSK. J7 with properties distinct from known cyclindependent kinases (cdks). Mouse p34psK. J3 shows less than 50% amino acid identity to p34-,~ 33~*~~, and p360dk3, lacks a PSTAIRE motif, and does not bind to p13* Uc’. Cyclin Dl-p34psK. J3 complexes accumulate in macrophages during Gl and decline in S phase, whereas complexes involving cyclins D2 and D3 form in proliferating T cells. Although histone Hl kinase activity is not detected in cyclin D or PSK-J3 immunoprecipitates, cyclin D-p34PSK-J3 complexes assembled in vitro stably bind and phosphorylate the retinoblastoma gene product (pRb) and an Rb-like protein (~ 107) but do not interact with pRb mutants that are functionally inactive. Thus, p34psK. J3 is a cyclin D-regulated catalytic subunit that acts as an Rb (but not Hi) kinase.
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