PMID- 10359609
OWN - NLM
STAT- MEDLINE
DCOM- 19990729
LR  - 20181113
IS  - 1059-1524 (Print)
IS  - 1059-1524 (Linking)
VI  - 10
IP  - 6
DP  - 1999 Jun
TI  - The PDZ domain of the LIM protein enigma binds to beta-tropomyosin.
PG  - 1973-84
AB  - PDZ and LIM domains are modular protein interaction motifs present in proteins
      with diverse functions. Enigma is representative of a family of proteins composed
      of a series of conserved PDZ and LIM domains. The LIM domains of Enigma and its
      most related family member, Enigma homology protein, bind to protein kinases,
      whereas the PDZ domains of Enigma and family member actin-associated LIM protein 
      bind to actin filaments. Enigma localizes to actin filaments in fibroblasts via
      its PDZ domain, and actin-associated LIM protein binds to and colocalizes with
      the actin-binding protein alpha-actinin-2 at Z lines in skeletal muscle. We show 
      that Enigma is present at the Z line in skeletal muscle and that the PDZ domain
      of Enigma binds to a skeletal muscle target, the actin-binding protein
      tropomyosin (skeletal beta-TM). The interaction between Enigma and skeletal
      beta-TM was specific for the PDZ domain of Enigma, was abolished by mutations in 
      the PDZ domain, and required the PDZ-binding consensus sequence (Thr-Ser-Leu) at 
      the extreme carboxyl terminus of skeletal beta-TM. Enigma interacted with
      isoforms of tropomyosin expressed in C2C12 myotubes and formed an
      immunoprecipitable complex with skeletal beta-TM in transfected cells. The
      association of Enigma with skeletal beta-TM suggests a role for Enigma as an
      adapter protein that directs LIM-binding proteins to actin filaments of muscle
      cells.
FAU - Guy, P M
AU  - Guy PM
AD  - Department of Medicine, University of California at San Diego, La Jolla,
      California 92093-0650, USA.
FAU - Kenny, D A
AU  - Kenny DA
FAU - Gill, G N
AU  - Gill GN
LA  - eng
GR  - T32 HL007770/HL/NHLBI NIH HHS/United States
GR  - DK-09320/DK/NIDDK NIH HHS/United States
GR  - T32HL-07770/HL/NHLBI NIH HHS/United States
GR  - 5PO 1 CA58689/CA/NCI NIH HHS/United States
GR  - F32 DK009320/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Biol Cell
JT  - Molecular biology of the cell
JID - 9201390
RN  - 0 (Actins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Cipp protein, mouse)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (LIM Domain Proteins)
RN  - 0 (Pdlim7 protein, mouse)
RN  - 0 (Peptide Fragments)
RN  - 0 (Protein Isoforms)
RN  - 0 (Tropomyosin)
SB  - IM
MH  - Actins/metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Carrier Proteins/*genetics/*metabolism
MH  - Cell Line
MH  - Cytoskeletal Proteins
MH  - Gene Expression Regulation, Developmental
MH  - *Intracellular Signaling Peptides and Proteins
MH  - LIM Domain Proteins
MH  - Mice
MH  - Molecular Sequence Data
MH  - Muscle, Skeletal/embryology/*metabolism
MH  - Mutation
MH  - Peptide Fragments/metabolism
MH  - Precipitin Tests
MH  - Protein Isoforms
MH  - Tropomyosin/*metabolism
PMC - PMC25398
EDAT- 1999/06/08 00:00
MHDA- 1999/06/08 00:01
CRDT- 1999/06/08 00:00
PHST- 1999/06/08 00:00 [pubmed]
PHST- 1999/06/08 00:01 [medline]
PHST- 1999/06/08 00:00 [entrez]
AID - 10.1091/mbc.10.6.1973 [doi]
PST - ppublish
SO  - Mol Biol Cell. 1999 Jun;10(6):1973-84. doi: 10.1091/mbc.10.6.1973.