PMID- 10362542
OWN - NLM
STAT- MEDLINE
DCOM- 19990902
LR  - 20220215
IS  - 0021-9533 (Print)
IS  - 0021-9533 (Linking)
VI  - 112 ( Pt 13)
DP  - 1999 Jul
TI  - Domain analysis of supervillin, an F-actin bundling plasma membrane protein with 
      functional nuclear localization signals.
PG  - 2125-36
AB  - A growing number of actin-associated membrane proteins have been implicated in
      motile processes, adhesive interactions, and signal transduction to the cell
      nucleus. We report here that supervillin, an F-actin binding protein originally
      isolated from bovine neutrophil plasma membranes, contains functional nuclear
      targeting signals and localizes at or near vinculin-containing focal adhesion
      plaques in COS7-2 and CV1 cells. Overexpression of full-length supervillin in
      these cells disrupts the integrity of focal adhesion plaques and results in
      increased levels of F-actin and vinculin. Localization studies of chimeric
      proteins containing supervillin sequences fused with the enhanced green
      fluorescent protein indicate that: (1) the amino terminus promotes F-actin
      binding, targeting to focal adhesions, and limited nuclear localization; (2) the 
      dominant nuclear targeting signal is in the center of the protein; and (3) the
      carboxy-terminal villin/gelsolin homology domain of supervillin does not, by
      itself, bind tightly to the actin cytoskeleton in vivo. Overexpression of
      chimeras containing both the amino-terminal F-actin binding site(s) and the
      dominant nuclear targeting signal results in the formation of large nuclear
      bundles containing F-actin, supervillin, and lamin. These results suggest that
      supervillin may contribute to cytoarchitecture in the nucleus, as well as at the 
      plasma membrane.
FAU - Wulfkuhle, J D
AU  - Wulfkuhle JD
AD  - Department of Cell Biology, University of Massachusetts Medical School,
      Worcester, MA 01605, USA.
FAU - Donina, I E
AU  - Donina IE
FAU - Stark, N H
AU  - Stark NH
FAU - Pope, R K
AU  - Pope RK
FAU - Pestonjamasp, K N
AU  - Pestonjamasp KN
FAU - Niswonger, M L
AU  - Niswonger ML
FAU - Luna, E J
AU  - Luna EJ
LA  - eng
GR  - R01 GM033048/GM/NIGMS NIH HHS/United States
GR  - 5T32HD07312-12/HD/NICHD NIH HHS/United States
GR  - GM33048/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - J Cell Sci
JT  - Journal of cell science
JID - 0052457
RN  - 0 (Actins)
RN  - 0 (DNA Primers)
RN  - 0 (Lamins)
RN  - 0 (Luminescent Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Nuclear Localization Signals)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 125361-02-6 (Vinculin)
RN  - 147336-22-9 (Green Fluorescent Proteins)
SB  - IM
MH  - Actins/*metabolism
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - COS Cells
MH  - Cattle
MH  - Cell Adhesion
MH  - Cell Line
MH  - Cytoskeleton/metabolism
MH  - DNA Primers/genetics
MH  - Gene Expression
MH  - Green Fluorescent Proteins
MH  - Lamins
MH  - Luminescent Proteins/genetics/metabolism
MH  - Membrane Proteins/*chemistry/genetics/*metabolism
MH  - Microfilament Proteins/*chemistry/genetics/*metabolism
MH  - Nuclear Localization Signals
MH  - Nuclear Proteins/metabolism
MH  - Phenotype
MH  - Recombinant Fusion Proteins/chemistry/genetics/metabolism
MH  - Vinculin/metabolism
EDAT- 1999/06/11 00:00
MHDA- 1999/06/11 00:01
CRDT- 1999/06/11 00:00
PHST- 1999/06/11 00:00 [pubmed]
PHST- 1999/06/11 00:01 [medline]
PHST- 1999/06/11 00:00 [entrez]
AID - 10.1242/jcs.112.13.2125 [doi]
PST - ppublish
SO  - J Cell Sci. 1999 Jul;112 ( Pt 13):2125-36. doi: 10.1242/jcs.112.13.2125.