PMID- 23079622
OWN - NLM
STAT- MEDLINE
DCOM- 20130325
LR  - 20211021
IS  - 1090-2104 (Electronic)
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 428
IP  - 3
DP  - 2012 Nov 23
TI  - Role of km23-1 in RhoA/actin-based cell migration.
PG  - 333-8
LID - S0006-291X(12)01984-5 [pii]
LID - 10.1016/j.bbrc.2012.10.047 [doi]
AB  - km23-1 was originally identified as a TGFss receptor-interacting protein that 
      plays an important role in TGFss signaling. Moreover, km23-1 is actually part of 
      an ancient superfamily of NTPase-regulatory proteins, widely represented in 
      archaea and bacteria. To further elucidate the function of km23-1, we identified 
      novel protein interacting partners for km23-1 by using tandem affinity 
      purification (TAP) and tandem mass spectrometry (MS). Here we show that km23-1 
      interacted with a class of proteins involved in actin-based cell motility and 
      modulation of the actin cytoskeleton. We further showed that km23-1 modulates the 
      formation of a highly organized stress fiber network. More significantly, we 
      demonstrated that knockdown (KD) of km23-1 decreased RhoA activation in Mv1Lu 
      epithelial cells. Finally, our results demonstrated for the first time that 
      depletion of km23-1 inhibited cell migration of human colon carcinoma cells 
      (HCCCs) in wound-healing assays. Overall, our findings demonstrate that km23-1 
      regulates RhoA and motility-associated actin modulating proteins, suggesting that 
      km23-1 may represent a novel target for anti-metastatic therapy.
CI  - Copyright (c) 2012 Elsevier Inc. All rights reserved.
FAU - Jin, Qunyan
AU  - Jin Q
AD  - Department of Biochemistry and Molecular Biology, Penn State Hershey College of 
      Medicine, PA 17033, USA.
FAU - Pulipati, Nageswara R
AU  - Pulipati NR
FAU - Zhou, Weidong
AU  - Zhou W
FAU - Staub, Cory M
AU  - Staub CM
FAU - Liotta, Lance A
AU  - Liotta LA
FAU - Mulder, Kathleen M
AU  - Mulder KM
LA  - eng
GR  - CA092889-08S1/CA/NCI NIH HHS/United States
GR  - CA092889/CA/NCI NIH HHS/United States
GR  - R01 CA092889/CA/NCI NIH HHS/United States
GR  - CA090765/CA/NCI NIH HHS/United States
GR  - R01 CA090765/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20121015
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Actins)
RN  - 0 (DYNLRB1 protein, human)
RN  - 124671-05-2 (RHOA protein, human)
RN  - EC 3.6.4.2 (Cytoplasmic Dyneins)
RN  - EC 3.6.5.2 (rhoA GTP-Binding Protein)
SB  - IM
MH  - Actins/*biosynthesis
MH  - *Cell Movement
MH  - Cytoplasmic Dyneins/genetics/*physiology
MH  - HCT116 Cells
MH  - HEK293 Cells
MH  - Humans
MH  - Neoplasm Metastasis/*pathology
MH  - Wound Healing
MH  - rhoA GTP-Binding Protein/*biosynthesis
PMC - PMC3513371
MID - NIHMS415186
EDAT- 2012/10/20 06:00
MHDA- 2013/03/26 06:00
PMCR- 2013/11/23
CRDT- 2012/10/20 06:00
PHST- 2012/10/06 00:00 [received]
PHST- 2012/10/09 00:00 [accepted]
PHST- 2012/10/20 06:00 [entrez]
PHST- 2012/10/20 06:00 [pubmed]
PHST- 2013/03/26 06:00 [medline]
PHST- 2013/11/23 00:00 [pmc-release]
AID - S0006-291X(12)01984-5 [pii]
AID - 10.1016/j.bbrc.2012.10.047 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2012 Nov 23;428(3):333-8. doi: 
      10.1016/j.bbrc.2012.10.047. Epub 2012 Oct 15.