PMID- 22665485
OWN - NLM
STAT- MEDLINE
DCOM- 20121018
LR  - 20211203
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 287
IP  - 30
DP  - 2012 Jul 20
TI  - Misshapen-like kinase 1 (MINK1) is a novel component of striatin-interacting 
      phosphatase and kinase (STRIPAK) and is required for the completion of 
      cytokinesis.
PG  - 25019-29
LID - 10.1074/jbc.M112.372342 [doi]
AB  - Cytokinesis is initiated by constriction of the cleavage furrow and terminated by 
      abscission of the intercellular bridge that connects two separating daughter 
      cells. The complicated processes of cytokinesis are coordinated by 
      phosphorylation and dephosphorylation mediated by protein kinases and 
      phosphatases. Mammalian Misshapen-like kinase 1 (MINK1) is a member of the 
      germinal center kinases and is known to regulate cytoskeletal organization and 
      oncogene-induced cell senescence. To search for novel regulators of cytokinesis, 
      we performed a screen using a library of siRNAs and found that MINK1 was 
      essential for cytokinesis. Time-lapse analysis revealed that MINK1-depleted cells 
      were able to initiate furrowing but that abscission was disrupted. STRN4 
      (Zinedin) is a regulatory subunit of protein phosphatase 2A (PP2A) and was 
      recently shown to be a component of a novel protein complex called 
      striatin-interacting phosphatase and kinase (STRIPAK). Mass spectrometry analysis 
      showed that MINK1 was a component of STRIPAK and that MINK1 directly interacted 
      with STRN4. Similar to MINK1 depletion, STRN4-knockdown induced multinucleated 
      cells and inhibited the completion of abscission. In addition, STRN4 reduced 
      MINK1 activity in the presence of catalytic and structural subunits of PP2A. Our 
      study identifies a novel regulatory network of protein kinases and phosphatases 
      that regulate the completion of abscission.
FAU - Hyodo, Toshinori
AU  - Hyodo T
AD  - Division of Cancer Biology, Nagoya University Graduate School of Medicine, Nagoya 
      466-8550, Japan.
FAU - Ito, Satoko
AU  - Ito S
FAU - Hasegawa, Hitoki
AU  - Hasegawa H
FAU - Asano, Eri
AU  - Asano E
FAU - Maeda, Masao
AU  - Maeda M
FAU - Urano, Takeshi
AU  - Urano T
FAU - Takahashi, Masahide
AU  - Takahashi M
FAU - Hamaguchi, Michinari
AU  - Hamaguchi M
FAU - Senga, Takeshi
AU  - Senga T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20120604
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Calmodulin-Binding Proteins)
RN  - 0 (Multienzyme Complexes)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (zinedin)
RN  - EC 2.7.11.1 (MINK1 protein, human)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 3.1.3.16 (PPP2CA protein, human)
RN  - EC 3.1.3.16 (Protein Phosphatase 2)
SB  - IM
MH  - Calmodulin-Binding Proteins/genetics/*metabolism
MH  - Cytokinesis/*physiology
MH  - Gene Knockdown Techniques
MH  - HeLa Cells
MH  - Humans
MH  - Multienzyme Complexes/genetics/*metabolism
MH  - Nerve Tissue Proteins/genetics/*metabolism
MH  - Protein Phosphatase 2/genetics/*metabolism
MH  - Protein Serine-Threonine Kinases/genetics/*metabolism
PMC - PMC3408143
EDAT- 2012/06/06 06:00
MHDA- 2012/10/19 06:00
PMCR- 2013/07/20
CRDT- 2012/06/06 06:00
PHST- 2012/06/06 06:00 [entrez]
PHST- 2012/06/06 06:00 [pubmed]
PHST- 2012/10/19 06:00 [medline]
PHST- 2013/07/20 00:00 [pmc-release]
AID - S0021-9258(20)73672-0 [pii]
AID - M112.372342 [pii]
AID - 10.1074/jbc.M112.372342 [doi]
PST - ppublish
SO  - J Biol Chem. 2012 Jul 20;287(30):25019-29. doi: 10.1074/jbc.M112.372342. Epub 
      2012 Jun 4.