Abstract:
:p21-activated protein kinase gamma-PAK phosphorylates prolactin (PRL) in rat pituitary secretory granules on Ser-177 and on the equivalent site, Ser-179, in recombinant human PRL. This is shown by comparison of phosphopeptide maps with the human PRL mutant S179D. gamma-PAK is present in rat and bovine granules as identified by in-gel phosphorylation of histone H4, and by immunoblotting. Thus, phosphorylation of PRL by gamma-PAK in granules produces the PRL molecule that has been shown to antagonize the growth-promoting activity of unmodified PRL, and is consistent with the identified role of gamma-PAK in the induction and maintenance of cytostasis.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Tuazon PT,Lorenson MY,Walker AM,Traugh JAdoi
10.1016/s0014-5793(02)02444-4keywords:
subject
Has Abstractpub_date
2002-03-27 00:00:00pages
84-8issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302024444journal_volume
515pub_type
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