JBC INTERFERin siRNA transfection reagent

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M005693200 on October 2, 2000

J. Biol. Chem., Vol. 276, Issue 1, 583-592, January 5, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/1/583    most recent
M005693200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by McElhinny, A. S.
Right arrow Articles by Gregorio, C. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McElhinny, A. S.
Right arrow Articles by Gregorio, C. C.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

The N-terminal End of Nebulin Interacts with Tropomodulin at the Pointed Ends of the Thin Filaments*

Abigail S. McElhinnyDagger , Bernhard Kolmerer§, Velia M. Fowler, Siegfried Labeit§, and Carol C. GregorioDagger ||**

From the Departments of Dagger  Cell Biology and Anatomy and || Cellular and Molecular Biology, University of Arizona, Tucson, Arizona 85724, the § European Molecular Biology Laboratory, Heidelberg 69012, Germany, and the  Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037

Strict regulation of actin thin filament length is critical for the proper functioning of sarcomeres, the basic contractile units of myofibrils. It has been hypothesized that a molecular template works with actin filament capping proteins to regulate thin filament lengths. Nebulin is a giant protein (~800 kDa) in skeletal muscle that has been proposed to act as a molecular ruler to specify the thin filament lengths characteristic of different muscles. Tropomodulin (Tmod), a pointed end thin filament capping protein, has been shown to maintain the final length of the thin filaments. Immunofluorescence microscopy revealed that the N-terminal end of nebulin colocalizes with Tmod at the pointed ends of thin filaments. The three extreme N-terminal modules (M1-M2-M3) of nebulin bind specifically to Tmod as demonstrated by blot overlay, bead binding, and solid phase binding assays. These data demonstrate that the N terminus of the nebulin molecule extends to the extreme end of the thin filament and also establish a novel biochemical function for this end. Two Tmod isoforms, erythrocyte Tmod (E-Tmod), expressed in embryonic and slow skeletal muscle, and skeletal Tmod (Sk-Tmod), expressed late in fast skeletal muscle differentiation, bind on overlapping sites to recombinant N-terminal nebulin fragments. Sk-Tmod binds nebulin with higher affinity than E-Tmod does, suggesting that the Tmod/nebulin interaction exhibits isoform specificity. These data provide evidence that Tmod and nebulin may work together as a linked mechanism to control thin filament lengths in skeletal muscle.

* This work was supported by the National Institutes of Health Grants HL57461 and HL03985 (to C. C. G.), HL07249 (to A. S. M.), and GM3425 (to V. M. F.), Deutsche Forschungsgemeinschaft Grant La 668/3-3 (to S. L.), and an award from the Human Frontier Science Program (to C. C. G., V. M. F., and S. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) X83957.

** To whom correspondence should be addressed: Dept. of Cell Biology and Anatomy, LSN455, The University of Arizona, 1501 N. Campbell Ave., Tucson, AZ 85724. Tel.: 520-626-8113; Fax: 520-626-2097; E-mail: gregorio@u.arizona.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
C. T. Pappas, N. Bhattacharya, J. A. Cooper, and C. C. Gregorio
Nebulin Interacts with CapZ and Regulates Thin Filament Architecture within the Z-Disc
Mol. Biol. Cell, May 1, 2008; 19(5): 1837 - 1847.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
M.-L. Bang, X. Li, R. Littlefield, S. Bremner, A. Thor, K. U. Knowlton, R. L. Lieber, and J. Chen
Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle
J. Cell Biol., June 19, 2006; 173(6): 905 - 916.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
A. S. McElhinny, C. Schwach, M. Valichnac, S. Mount-Patrick, and C. C. Gregorio
Nebulin regulates the assembly and lengths of the thin filaments in striated muscle
J. Cell Biol., September 12, 2005; 170(6): 947 - 957.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
N. J. Greenfield, A. S. Kostyukova, and S. E. Hitchcock-DeGregori
Structure and Tropomyosin Binding Properties of the N-Terminal Capping Domain of Tropomodulin 1
Biophys. J., January 1, 2005; 88(1): 372 - 383.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
K. L. Fritz-Six, P. R. Cox, R. S. Fischer, B. Xu, C. C. Gregorio, H. Y. Zoghbi, and V. M. Fowler
Aberrant myofibril assembly in tropomodulin1 null mice leads to aborted heart development and embryonic lethality
J. Cell Biol., December 8, 2003; 163(5): 1033 - 1044.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
V. M. Fowler, N. J. Greenfield, and J. Moyer
Tropomodulin Contains Two Actin Filament Pointed End-capping Domains
J. Biol. Chem., October 10, 2003; 278(41): 40000 - 40009.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
R. E. Mudry, C. N. Perry, M. Richards, V. M. Fowler, and C. C. Gregorio
The interaction of tropomodulin with tropomyosin stabilizes thin filaments in cardiac myocytes
J. Cell Biol., September 15, 2003; 162(6): 1057 - 1068.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
K. Sudre, C. Leroux, G. Pietu, I. Cassar-Malek, E. Petit, A. Listrat, C. Auffray, B. Picard, P. Martin, and J.-F. Hocquette
Transcriptome Analysis of Two Bovine Muscles during Ontogenesis
J. Biochem., June 1, 2003; 133(6): 745 - 756.
[Abstract] [Full Text] [PDF]

Home page
 J. Nutr.Home page
R. J. Hunter, C. Neagoe, H. A. Jarvelainen, C. R. Martin, K. O. Lindros, W. A. Linke, and V. R. Preedy
Alcohol Affects the Skeletal Muscle Proteins, Titin and Nebulin in Male and Female Rats
J. Nutr., April 1, 2003; 133(4): 1154 - 1157.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
A. Kontrogianni-Konstantopoulos, E. M. Jones, D. B. van Rossum, and R. J. Bloch
Obscurin Is a Ligand for Small Ankyrin 1 in Skeletal Muscle
Mol. Biol. Cell, March 1, 2003; 14(3): 1138 - 1148.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
O. Ogut, M. M. Hossain, and J.-P. Jin
Interactions between Nebulin-like Motifs and Thin Filament Regulatory Proteins
J. Biol. Chem., January 24, 2003; 278(5): 3089 - 3097.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
I. Krieger, A. Kostyukova, A. Yamashita, Y. Nitanai, and Y. Maeda
Crystal Structure of the C-Terminal Half of Tropomodulin and Structural Basis of Actin Filament Pointed-End Capping
Biophys. J., November 1, 2002; 83(5): 2716 - 2725.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.