Home LiteratureArticle Details
PMID: 6405378 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma.

Pardo JV, Siliciano JD, Craig SW

Abstract

We have found that vinculin is localized at the sarcolemma of skeletal muscle cells in a two-dimensional orthogonal lattice. Perpendicular to the longitudinal axis of the cell, bands of vinculin encircle the muscle cell and repeat along its length with a periodicity corresponding to the subjacent sarcomeres. Because of their appearance and probable function, we call the transverse elements of the lattice "costameres" (Latin costa, rib; Greek meros, part). Costameres have a substructure consisting of densely clustered patches of vinculin; the patches are segregated into two rows which flank the Z line and overlie the I band of the underlying sarcomere. It is likely that the costameres are physically coupled to the underlying myofibrils because: (i) the costameres broaden and narrow in concert with the underlying I band in stretched and contracted muscle, and (ii) adjacent but misaligned myofibrils are mirrored by corresponding discontinuities in the overlying costameres. We hypothesize that the sarcolemmal lattice, detected because vinculin is one of its molecular components, integrates the contractile apparatus with the sarcolemma during lengthening and shortening of the muscle cells.

MeSH Terms
Actins/metabolism Animals Chickens Cytoskeleton/ultrastructure Fluorescent Antibody Technique Molecular Weight Muscle Contraction Muscle Proteins/metabolism Muscles/ultrastructure Protein Binding Sarcolemma/metabolism Vinculin
Chemicals
Actins Muscle Proteins Vinculin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Pardo J V
Siliciano J D
Craig S W
References (22)
22 references, click to expand
  1. A 130K protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured chicken cells.
    Cell. 1979 Sep;18(1):193-205 PMID: 574428
  2. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
    Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350-4 PMID: 388439
  3. Vinculin, an intracellular protein localized at specialized sites where microfilament bundles terminate at cell membranes.
    Proc Natl Acad Sci U S A. 1980 Jul;77(7):4127-31 PMID: 6776523
  4. A transmembrane relationship between fibronectin and vinculin (130 kd protein): serum modulation in normal and transformed hamster fibroblasts.
    Cell. 1981 May;24(2):481-92 PMID: 6786758
  5. A simple method of reducing the fading of immunofluorescence during microscopy.
    J Immunol Methods. 1981;43(3):349-50 PMID: 7019347
  6. Interaction of alpha-actinin and vinculin with actin: opposite effects on filament network formation.
    Proc Natl Acad Sci U S A. 1981 May;78(5):3005-9 PMID: 6789327
  7. The structure of smooth and striated portions of the adductor muscle of the valves in a scallop.
    J Ultrastruct Res. 1981 Aug;76(2):134-48 PMID: 7197728
  8. Immunoelectron microscope studies of membrane-microfilament interactions: distributions of alpha-actinin, tropomyosin, and vinculin in intestinal epithelial brush border and chicken gizzard smooth muscle cells.
    J Cell Biol. 1981 Dec;91(3 Pt 1):614-28 PMID: 6799520
  9. Primary role of sarcoplasmic reticulum in phasic contractile activation of cardiac myocytes with shunted myolemma.
    J Cell Biol. 1981 Dec;91(3 Pt 1):728-42 PMID: 6276409
  10. Association of fibronectin and vinculin with focal contacts and stress fibers in stationary hamster fibroblasts.
    J Cell Biol. 1982 Feb;92(2):398-408 PMID: 6801062
  11. Ultrastructure of chicken cardiac muscle as studied by double immunolabeling in electron microscopy.
    Proc Natl Acad Sci U S A. 1981 Dec;78(12):7619-23 PMID: 6801654
  12. High-affinity interaction of vinculin with actin filaments in vitro.
    Cell. 1982 Jan;28(1):83-90 PMID: 6802502
  13. Co-existence of vinculin and a vinculin-like protein of higher molecular weight in smooth muscle.
    J Biol Chem. 1982 Sep 25;257(18):11024-31 PMID: 6809764
  14. Preparation of smooth muscle alpha-actinin.
    Methods Enzymol. 1982;85 Pt B:316-21 PMID: 7121272
  15. Meta-vinculin--a vinculin-related protein with solubility properties of a membrane protein.
    Nature. 1982 Dec 9;300(5892):533-5 PMID: 6815540
  16. An experimental study of the non-fibrillar components in frog striated muscle.
    Bull Johns Hopkins Hosp. 1958 Dec;103(6):267-80 PMID: 13608165
  17. Inter-Z bridges in the flight muscle of the bee.
    J Ultrastruct Res. 1965 Dec;13(5):435-43 PMID: 5848840
  18. Structure and some contractile properties of fast and slow muscles of the chicken.
    J Physiol. 1969 Nov;205(1):131-45 PMID: 5347713
  19. Peripheral couplings in adult vertebrate skeletal muscle. Anatomical observations and functional implications.
    J Cell Biol. 1974 Jul;62(1):223-7 PMID: 4600885
  20. SDS microslab linear gradient polyacrylamide gel electrophoresis.
    Anal Biochem. 1978 Jul 1;87(2):386-96 PMID: 686359
  21. alpha-Actinin localization in the junctional complex of intestinal epithelial cells.
    J Cell Biol. 1979 Jan;80(1):203-10 PMID: 370125
  22. Microinjection and localization of a 130K protein in living fibroblasts: a relationship to actin and fibronectin.
    Cell. 1980 Mar;19(3):587-95 PMID: 6988083
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1983-02-00
Pages
1008-12
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC393517
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]