PMID- 21160029
OWN - NLM
STAT- MEDLINE
DCOM- 20110420
LR  - 20211203
IS  - 1522-1563 (Electronic)
IS  - 0363-6143 (Linking)
VI  - 300
IP  - 3
DP  - 2011 Mar
TI  - Phosphorylation of radixin regulates cell polarity and Mrp-2 distribution in 
      hepatocytes.
PG  - C416-24
LID - 10.1152/ajpcell.00467.2010 [doi]
AB  - Radixin, the dominant ezrin-radixin-moesin (ERM) protein in hepatocytes, has two 
      important binding domains: an NH(2)-terminal region that binds to plasma membrane 
      and a COOH-terminal region that binds to F-actin after a conformational 
      activation by phosphorylation at Thr564. The present studies were undertaken to 
      investigate the cellular changes in expression of radixin in WIF-B cells and to 
      assess radixin distribution and its influence on cell polarity. We used a 
      recombinant adenoviral expression system encoding radixin wild-type and Thr564 
      mutants fused to cyan fluorescent protein (CFP), as well as conventional 
      immunostaining procedures. Functional analyses were characterized quantitatively. 
      Similar to endogenous radixin, adenovirus-infected radixin-CFP-wild type and 
      nonphosphorylatable radixin-CFP-T564A were found to be expressed heavily in the 
      compartment of canalicular membrane vacuoles, typically colocalizing with 
      multidrug resistance-associated protein 2 (Mrp-2). Expression of 
      radixin-CFP-T564D, which mimics constant phosphorylation, was quite different, 
      being rarely associated with canalicular membranes. The WIF-B cells were devoid 
      of a secretory response, T567D radixin became predominantly redistributed to the 
      basolateral membrane, usually in the form of dense, long spikes and fingerlike 
      projections, and the altered cell polarity involved changes in apical membrane 
      markers. Differences in polar distribution of radixin suggest a role for the 
      linker protein in promoting formation and plasticity of membrane surface 
      projections and also suggest that radixin might be an organizer and regulator of 
      Mrp-2 and cell polarity in hepatocytes.
FAU - Suda, Jo
AU  - Suda J
AD  - Keck School of Medicine, Division of Gastrointestinal & Liver Diseases, Univ. of 
      Southern California, Zonal Ave., HMR 101, Los Angeles, CA 90033, USA.
FAU - Zhu, Lixin
AU  - Zhu L
FAU - Karvar, Serhan
AU  - Karvar S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20101215
PL  - United States
TA  - Am J Physiol Cell Physiol
JT  - American journal of physiology. Cell physiology
JID - 100901225
RN  - 0 (ABCC2 protein, human)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Multidrug Resistance-Associated Protein 2)
RN  - 0 (Multidrug Resistance-Associated Proteins)
RN  - 0 (Mutant Proteins)
RN  - 144517-21-5 (radixin)
SB  - IM
MH  - Animals
MH  - Cell Line, Tumor
MH  - Cell Polarity/*physiology
MH  - Cell Surface Extensions/metabolism
MH  - Cytoskeletal Proteins/genetics/*metabolism
MH  - Genetic Vectors/genetics
MH  - Hepatocytes/cytology/*metabolism
MH  - Humans
MH  - Hybridomas
MH  - Membrane Proteins/genetics/*metabolism
MH  - Multidrug Resistance-Associated Protein 2
MH  - Multidrug Resistance-Associated Proteins/*metabolism
MH  - Mutant Proteins/genetics
MH  - Phosphorylation/genetics
MH  - Rats
MH  - Transfection
MH  - Vacuoles/metabolism
EDAT- 2010/12/17 06:00
MHDA- 2011/04/22 06:00
CRDT- 2010/12/17 06:00
PHST- 2010/12/17 06:00 [entrez]
PHST- 2010/12/17 06:00 [pubmed]
PHST- 2011/04/22 06:00 [medline]
AID - ajpcell.00467.2010 [pii]
AID - 10.1152/ajpcell.00467.2010 [doi]
PST - ppublish
SO  - Am J Physiol Cell Physiol. 2011 Mar;300(3):C416-24. doi: 
      10.1152/ajpcell.00467.2010. Epub 2010 Dec 15.