PMID- 10098932
OWN - NLM
STAT- MEDLINE
DCOM- 19990603
LR  - 20061115
IS  - 0886-1544 (Print)
IS  - 0886-1544 (Linking)
VI  - 42
IP  - 3
DP  - 1999
TI  - Activities of the EM10 protein from Echinococcus multilocularis in cultured 
      mammalian cells demonstrate functional relationships to ERM family members.
PG  - 178-88
AB  - The ezrin-radixin-moesin (ERM) homolog EM10 is expressed by the larval stage of 
      the parasite E. multilocularis and shows 46.9% overall identity in the primary 
      structure with human ezrin. To determine whether EM10 has similar activities to 
      ERM proteins, we investigated properties of the protein expressed in mammalian 
      cells. In particular, we transiently expressed haemagglutinin-tagged (HA-tagged) 
      versions of the full-length EM10 as well as the amino- and the carboxy-terminal 
      halves of EM10 in HtTA-1 cells. In addition we stably transfected NIH-3T3 cells 
      with untagged full-length EM10. The data demonstrate that EM10 polypeptides 
      behave like their corresponding portions of radixin when transiently expressed in 
      mammalian cells. The full-length and amino-terminal EM10 polypeptides were 
      localized to cortical structures. Cells expressing the carboxy-terminal 
      polypeptide of EM10 showed long actin-filled protrusions. Cells expressing 
      full-length EM10 showed a reduction in endogenous moesin-staining at cortical 
      structures. In stably transfected NIH-3T3 cells EM10 was not crisply localized 
      but rather was diffuse throughout the cytoplasm. These cells showed a conspicuous 
      loss of stress-fibers, a phenotype that was not seen in analogous experiments 
      with ERM proteins. The results demonstrate both similarities and differences 
      between the functional properties of EM10 and ERM proteins expressed in 
      vertebrate cells.
FAU - Hubert, K
AU  - Hubert K
AD  - Institut fur Hygiene und Mikrobiologie, Universitat Wurzburg, Germany. 
      khubert@hygiene.uni-wuerzburg.de
FAU - Cordero, E
AU  - Cordero E
FAU - Frosch, M
AU  - Frosch M
FAU - Solomon, F
AU  - Solomon F
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cell Motil Cytoskeleton
JT  - Cell motility and the cytoskeleton
JID - 8605339
RN  - 0 (Actins)
RN  - 0 (Antigens, Helminth)
RN  - 0 (Antigens, Surface)
RN  - 0 (Blood Proteins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (DNA Primers)
RN  - 0 (Elp protein, Echinococcus multilocularis)
RN  - 0 (Membrane Proteins)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (ezrin)
RN  - 144131-77-1 (moesin)
RN  - 144517-21-5 (radixin)
RN  - 17466-45-4 (Phalloidine)
SB  - IM
MH  - 3T3 Cells
MH  - Actins/metabolism
MH  - Animals
MH  - Antigens, Helminth/classification/immunology/*metabolism
MH  - Antigens, Surface/classification/immunology/*metabolism
MH  - Blood Proteins/metabolism
MH  - Blotting, Western
MH  - Cells, Cultured
MH  - *Cytoskeletal Proteins
MH  - DNA Primers
MH  - Echinococcus/*metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Membrane Proteins/metabolism
MH  - Mice
MH  - Microfilament Proteins/immunology/metabolism
MH  - Microscopy, Fluorescence
MH  - Microvilli/metabolism
MH  - Phalloidine/metabolism
MH  - Phosphoproteins/metabolism
MH  - Pseudopodia/metabolism
MH  - Transfection
EDAT- 1999/03/31 03:05
MHDA- 2000/06/20 09:00
CRDT- 1999/03/31 03:05
PHST- 1999/03/31 03:05 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1999/03/31 03:05 [entrez]
AID - 10.1002/(SICI)1097-0169(1999)42:3<178::AID-CM2>3.0.CO;2-3 [pii]
AID - 10.1002/(SICI)1097-0169(1999)42:3<178::AID-CM2>3.0.CO;2-3 [doi]
PST - ppublish
SO  - Cell Motil Cytoskeleton. 1999;42(3):178-88. doi: 
      10.1002/(SICI)1097-0169(1999)42:3<178::AID-CM2>3.0.CO;2-3.