PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163.

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Citation

Palmer RH, Schonwasser DC, Rahman D, Pappin DJ, Herget T, Parker PJ

PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163.

FEBS Lett. 1996 Jan 15;378(3):281-5.

PubMed ID
8557118 [ View in PubMed
]
Abstract

The 80kDa Myristolated Alanine-Rich C-Kinase Substrate (MARCKS) is a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid-activated PKC-related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro. Thus, control of MARCKS phosphorylation on these previously identified 'PKC' sites may be regulated under certain circumstances by PRK as well as PKC mediated signalling pathways. The implications for MARCKS as a marker of PKC activation and as a point of signal convergence are discussed.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Serine/threonine-protein kinase N1Q16512Details