PUBLICATION

Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in skeletal muscle

Authors
Almenar-Queralt, A., Lee, A., Conley, C.A., Ribas-Pouplana, L., and Fowler, V.M.
ID
ZDB-PUB-000406-1
Date
1999
Source
The Journal of biological chemistry   274(40): 28466-28475 (Journal)
Registered Authors
Conley, Catharine A.
Keywords
none
MeSH Terms
  • Actins/metabolism*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Carrier Proteins/genetics
  • Carrier Proteins/metabolism*
  • Chick Embryo
  • Chickens
  • DNA, Complementary
  • Microfilament Proteins*
  • Molecular Sequence Data
  • Muscle Development
  • Muscle, Skeletal/growth & development
  • Muscle, Skeletal/metabolism*
  • Protein Isoforms/genetics
  • Protein Isoforms/metabolism*
  • Sequence Homology, Amino Acid
  • Spectrin/metabolism
  • Tropomodulin
PubMed
10497209 Full text @ J. Biol. Chem.
Abstract
Tropomodulin (E-Tmod) is an actin filament pointed end capping protein that maintains the length of the sarcomeric actin filaments in striated muscle. Here, we describe the identification and characterization of a novel tropomodulin isoform, skeletal tropomodulin (Sk-Tmod) from chickens. Sk-Tmod is 62% identical in amino acid sequence to the previously described chicken E-Tmod and is the product of a different gene. Sk-Tmod isoform sequences are highly conserved across vertebrates and constitute an independent group in the tropomodulin family. In vitro, chicken Sk-Tmod caps actin and tropomyosin-actin filament pointed ends to the same extent as does chicken E-Tmod. However, E- and Sk-Tmods differ in their tissue distribution; Sk-Tmod predominates in fast skeletal muscle fibers, lens, and erythrocytes, while E-Tmod is found in heart and slow skeletal muscle fibers. Additionally, their expression is developmentally regulated during chicken breast muscle differentiation with Sk-Tmod replacing E-Tmod after hatching. Finally, in skeletal muscle fibers that coexpress both Sk- and E-Tmod, they are recruited to different actin filament-containing cytoskeletal structures within the cell: myofibrils and costameres, respectively. All together, these observations support the hypothesis that vertebrates have acquired different tropomodulin isoforms that play distinct roles in vivo.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping