PMID- 10329716
OWN - NLM
STAT- MEDLINE
DCOM- 19990709
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 21
DP  - 1999 May 21
TI  - Regulated interaction of protein kinase Cdelta with the heterogeneous nuclear
      ribonucleoprotein K protein.
PG  - 15101-9
AB  - The heterogeneous nuclear ribonucleoprotein (hnRNP) K protein recruits a
      diversity of molecular partners that are involved in signal transduction,
      transcription, RNA processing, and translation. K protein is phosphorylated in
      vivo and in vitro by inducible kinase(s) and contains several potential sites for
      protein kinase C (PKC) phosphorylation. In this study we show that K protein is
      phosphorylated in vitro by PKCdelta and by other PKCs. Deletion analysis and
      site-directed mutagenesis revealed that Ser302 is a major K protein site
      phosphorylated by PKCdelta in vitro. This residue is located in the middle of a
      short amino acid fragment that divides the two clusters of SH3-binding domains.
      Mutation of Ser302 decreased the level of phosphorylation of exogenously
      expressed K protein in phorbol 12-myristate 13-acetate-treated COS cells,
      suggesting that Ser302 is also a site for PKC-mediated phosphorylation in vivo.
      In vitro, PKCdelta binds K protein via the highly interactive KI domain, an
      interaction that is blocked by poly(C) RNA. Mutation of Ser302 did not alter the 
      K protein-PKCdelta interaction in vitro, suggesting that phosphorylation of this 
      residue alone is not sufficient to alter this interaction. Instead, binding of
      PKCdelta to K protein in vitro and in vivo was greatly increased by K protein
      phosphorylation on tyrosine residues. The ability of PKCdelta to bind and
      phosphorylate K protein may serve not only to alter the activity of K protein
      itself, but K protein may also bridge PKCdelta to other K protein molecular
      partners and thus facilitate molecular cross-talk. The regulated nature of the
      PKCdelta-K protein interaction may serve to meet cellular needs at sites of
      active transcription, RNA processing and translation in response to changing
      extracellular environment.
FAU - Schullery, D S
AU  - Schullery DS
AD  - Department of Medicine, University of Washington, Seattle, Washington 98195, USA.
FAU - Ostrowski, J
AU  - Ostrowski J
FAU - Denisenko, O N
AU  - Denisenko ON
FAU - Stempka, L
AU  - Stempka L
FAU - Shnyreva, M
AU  - Shnyreva M
FAU - Suzuki, H
AU  - Suzuki H
FAU - Gschwendt, M
AU  - Gschwendt M
FAU - Bomsztyk, K
AU  - Bomsztyk K
LA  - eng
GR  - DK45978/DK/NIDDK NIH HHS/United States
GR  - GM45134/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Heterogeneous-Nuclear Ribonucleoprotein K)
RN  - 0 (Heterogeneous-Nuclear Ribonucleoproteins)
RN  - 0 (Isoenzymes)
RN  - 0 (RNA, Heterogeneous Nuclear)
RN  - 0 (Ribonucleoproteins)
RN  - 452VLY9402 (Serine)
RN  - 63231-63-0 (RNA)
RN  - EC 2.7.1.- (Prkcd protein, mouse)
RN  - EC 2.7.11.13 (Protein Kinase C)
RN  - EC 2.7.11.13 (Protein Kinase C-delta)
SB  - IM
MH  - Animals
MH  - Cells, Cultured
MH  - Heterogeneous-Nuclear Ribonucleoprotein K
MH  - Heterogeneous-Nuclear Ribonucleoproteins
MH  - Isoenzymes/*metabolism
MH  - Mice
MH  - Mutation
MH  - Phosphorylation
MH  - Protein Kinase C/*metabolism
MH  - Protein Kinase C-delta
MH  - RNA/genetics
MH  - RNA, Heterogeneous Nuclear/genetics/*metabolism
MH  - Ribonucleoproteins/genetics/*metabolism
MH  - Serine/genetics/physiology
EDAT- 1999/05/18 00:00
MHDA- 1999/05/18 00:01
CRDT- 1999/05/18 00:00
PHST- 1999/05/18 00:00 [pubmed]
PHST- 1999/05/18 00:01 [medline]
PHST- 1999/05/18 00:00 [entrez]
AID - 10.1074/jbc.274.21.15101 [doi]
AID - S0021-9258(19)73197-4 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 May 21;274(21):15101-9. doi: 10.1074/jbc.274.21.15101.