PMID- 15242805
OWN - NLM
STAT- MEDLINE
DCOM- 20040917
LR  - 20220227
IS  - 0012-1606 (Print)
IS  - 0012-1606 (Linking)
VI  - 272
IP  - 1
DP  - 2004 Aug 1
TI  - The C. elegans ezrin-radixin-moesin protein ERM-1 is necessary for apical 
      junction remodelling and tubulogenesis in the intestine.
PG  - 262-76
AB  - Members of the ezrin-radixin-moesin (ERM) family of proteins have been found to 
      serve as linkers between membrane proteins and the F-actin cytoskeleton in many 
      organisms. We used RNA interference (RNAi) approach to assay ERM proteins of the 
      Caenorhabditis elegans genome for a possible involvement in apical junction (AJ) 
      assembly or positioning. We identify erm-1 as the only ERM protein required for 
      development and show, by multiple RNA interference, that additional four-point 
      one, ezrin-radixin-moesin (FERM) domain-containing proteins cannot compensate for 
      the depletion of ERM-1. ERM-1 is expressed in most if not all cells of the embryo 
      at low levels but is upregulated in epithelia, like the intestine. ERM-1 protein 
      co-localizes with F-actin and the intermediate filament protein IFB-2 at the 
      apical cell cortex. ERM-1 depletion results in intestine-specific phenotypes like 
      lumenal constrictions or even obstructions. This phenotype arises after 
      epithelial polarization of intestinal cells and can be monitored using markers of 
      the apical junction. We show that the initial steps of epithelial polarization in 
      the intestine are not affected in erm-1(RNAi) embryos but the positioning of 
      apical junction proteins to an apico-lateral position arrests prematurely or 
      fails, resulting in multiple obstructions of the intestinal flow after hatching. 
      Mechanistically, this phenotype might be due to an altered apical cytoskeleton 
      because the apical enrichment of F-actin filaments is lost specifically in the 
      intestine. ERM-1 is the first protein of the apical membrane domain affecting 
      junction remodelling in C. elegans. ERM-1 interacts genetically with the 
      catenin-cadherin system but not with the DLG-1 (Discs large)-dependent 
      establishment of the apical junction.
FAU - Van Furden, Daniela
AU  - Van Furden D
AD  - Institut fur Genetik, Heinrich-Heine-Universitat Dusseldorf, D-40225, Germany.
FAU - Johnson, Kevin
AU  - Johnson K
FAU - Segbert, Christoph
AU  - Segbert C
FAU - Bossinger, Olaf
AU  - Bossinger O
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Dev Biol
JT  - Developmental biology
JID - 0372762
RN  - 0 (Actins)
RN  - 0 (Blood Proteins)
RN  - 0 (Caenorhabditis elegans Proteins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (ERM-1 protein, C elegans)
RN  - 0 (Membrane Proteins)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (ezrin)
RN  - 144131-77-1 (moesin)
RN  - 144517-21-5 (radixin)
SB  - IM
MH  - Actins/genetics/metabolism/ultrastructure
MH  - Amino Acid Sequence
MH  - Animals
MH  - Blood Proteins/genetics/metabolism
MH  - Caenorhabditis elegans/embryology/growth & development
MH  - Caenorhabditis elegans Proteins/genetics/*metabolism
MH  - Cytoskeletal Proteins/genetics/*metabolism
MH  - Embryo, Nonmammalian
MH  - Epithelial Cells/metabolism/pathology
MH  - Gene Expression Regulation, Developmental
MH  - Intestinal Mucosa/metabolism
MH  - Intestines/*cytology/embryology/pathology
MH  - Membrane Proteins/genetics/metabolism
MH  - Microfilament Proteins/genetics/metabolism
MH  - Molecular Sequence Data
MH  - Phosphoproteins/genetics/metabolism
EDAT- 2004/07/10 05:00
MHDA- 2004/09/21 05:00
CRDT- 2004/07/10 05:00
PHST- 2003/08/04 00:00 [received]
PHST- 2004/03/24 00:00 [revised]
PHST- 2004/05/02 00:00 [accepted]
PHST- 2004/07/10 05:00 [pubmed]
PHST- 2004/09/21 05:00 [medline]
PHST- 2004/07/10 05:00 [entrez]
AID - S0012160604003562 [pii]
AID - 10.1016/j.ydbio.2004.05.012 [doi]
PST - ppublish
SO  - Dev Biol. 2004 Aug 1;272(1):262-76. doi: 10.1016/j.ydbio.2004.05.012.