PMID- 10644754
OWN - NLM
STAT- MEDLINE
DCOM- 20000229
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 4
DP  - 2000 Jan 28
TI  - A protein kinase from neutrophils that specifically recognizes Ser-3 in cofilin.
PG  - 2869-76
AB  - Cofilin promotes the depolymerization of actin filaments, which is required for a
      variety of cellular responses such as the formation of lamellipodia and
      chemotaxis. Phosphorylation of cofilin on serine residue 3 is known to block
      these activities. We now report that neutrophils contain a protein kinase that
      selectively catalyzes the phosphorylation of cofilin on serine 3 (>/=70%) and a
      nonspecific kinase that recognizes multiple sites in this protein. The selective 
      serine 3 cofilin kinase binds to a deoxyribonuclease I affinity column, whereas
      the nonspecific cofilin kinase does not. Deoxyribonuclease I forms a very tight
      complex with actin, and deoxyribonuclease affinity columns have been utilized to 
      identify a variety of proteins that interact with the cytoskeleton. The serine 3 
      cofilin kinase did not react with antibodies to LIM kinase 1 or 2, which can
      catalyze the phosphorylation of cofilin in other cell types. The activity of the 
      serine 3 cofilin kinase was insensitive to a variety of selective antagonists of 
      protein kinases but was blocked by staurosporine. This pattern of inhibition is
      similar to that observed for the kinase that is active with cofilin in intact
      neutrophils. Thus, neutrophils contain a protein kinase distinct from LIM
      kinase-1/2 that selectively recognizes serine 3 in cofilin.
FAU - Lian, J P
AU  - Lian JP
AD  - Center for Experimental Therapeutics and Reperfusion Injury, Brigham and Women's 
      Hospital, Boston, Massachusetts 02115, USA.
FAU - Marks, P G
AU  - Marks PG
FAU - Wang, J Y
AU  - Wang JY
FAU - Falls, D L
AU  - Falls DL
FAU - Badwey, J A
AU  - Badwey JA
LA  - eng
GR  - AI 23323/AI/NIAID NIH HHS/United States
GR  - DK 50015/DK/NIDDK NIH HHS/United States
GR  - K08 HL-03235/HL/NHLBI NIH HHS/United States
GR  - etc.
PT  - Journal Article
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 (Actin Depolymerizing Factors)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 452VLY9402 (Serine)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.11.1 (LIMK1 protein, human)
RN  - EC 2.7.11.1 (Lim Kinases)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
SB  - IM
MH  - Actin Depolymerizing Factors
MH  - Amino Acid Sequence
MH  - Animals
MH  - Catalysis
MH  - DNA-Binding Proteins/metabolism
MH  - Guinea Pigs
MH  - Humans
MH  - Lim Kinases
MH  - Microfilament Proteins/chemistry/*metabolism
MH  - Molecular Sequence Data
MH  - Neutrophils/*enzymology
MH  - Phosphorylation
MH  - Protein Kinases/isolation & purification/*metabolism
MH  - Protein-Serine-Threonine Kinases/metabolism
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Serine/*metabolism
MH  - Substrate Specificity
EDAT- 2000/01/25 09:00
MHDA- 2000/03/04 09:00
CRDT- 2000/01/25 09:00
PHST- 2000/01/25 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 2000/01/25 09:00 [entrez]
AID - 10.1074/jbc.275.4.2869 [doi]
AID - S0021-9258(18)31049-4 [pii]
PST - ppublish
SO  - J Biol Chem. 2000 Jan 28;275(4):2869-76. doi: 10.1074/jbc.275.4.2869.