Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins

Norbert Frey, Eric N. Olson

Research output: Contribution to journalArticle

137 Citations (Scopus)

Abstract

The Z-disc is a highly specialized multiprotein complex of striated muscles that serves as the interface of the sarcomere and the cytoskeleton. In addition to its role in muscle contraction, its juxtaposition to the plasma membrane suggests additional functions of the Z-disc in sensing and transmitting external and internal signals. Recently, we described two novel striated muscle-specific proteins, calsarcin-1 and calsarcin-2, that bind α-actinin on the Z-disc and serve as intracellular binding proteins for calcineurin, a calcium/calmodulindependent phosphatase shown to be integral in cardiac hypertrophy as well as skeletal muscle differentiation and fiber-type specification. Here, we describe an additional member of the calsarcin family, calsarcin-3, which is expressed specifically in skeletal muscle and is enriched in fast-twitch muscle fibers. Like calsarcin-1 and calsarcin-2, calsarcin-3 interacts with calcineurin, and the Z-disc proteins α-actinin, γ-filamin, and telethonin. In addition, we show that calsarcins interact with the PDZ-LIM domain protein ZASP/Cypher/Oracle, which also localizes to the Z-disc. Calsarcins represent a novel family of sarcomeric proteins that serve as focal points for the interactions of an array of proteins involved in Z-disc structure and signal transduction in striated muscle.

Original languageEnglish (US)
Pages (from-to)13998-14004
Number of pages7
JournalJournal of Biological Chemistry
Volume277
Issue number16
DOIs
StatePublished - Apr 19 2002

Fingerprint

Striated Muscle
Actinin
Muscle
Skeletal Muscle
Calcineurin
LIM Domain Proteins
Filamins
Fast-Twitch Muscle Fibers
PDZ Domains
Multiprotein Complexes
Protein Array Analysis
Sarcomeres
Proteins
Muscle Proteins
Skeletal Muscle Fibers
Cardiomegaly
Muscle Contraction
Cytoskeleton
Phosphoric Monoester Hydrolases
Signal Transduction

ASJC Scopus subject areas

  • Biochemistry

Cite this

Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins. / Frey, Norbert; Olson, Eric N.

In: Journal of Biological Chemistry, Vol. 277, No. 16, 19.04.2002, p. 13998-14004.

Research output: Contribution to journalArticle

@article{b9587582c7b145a9aaaa49c65fd3077a,
title = "Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins",
abstract = "The Z-disc is a highly specialized multiprotein complex of striated muscles that serves as the interface of the sarcomere and the cytoskeleton. In addition to its role in muscle contraction, its juxtaposition to the plasma membrane suggests additional functions of the Z-disc in sensing and transmitting external and internal signals. Recently, we described two novel striated muscle-specific proteins, calsarcin-1 and calsarcin-2, that bind α-actinin on the Z-disc and serve as intracellular binding proteins for calcineurin, a calcium/calmodulindependent phosphatase shown to be integral in cardiac hypertrophy as well as skeletal muscle differentiation and fiber-type specification. Here, we describe an additional member of the calsarcin family, calsarcin-3, which is expressed specifically in skeletal muscle and is enriched in fast-twitch muscle fibers. Like calsarcin-1 and calsarcin-2, calsarcin-3 interacts with calcineurin, and the Z-disc proteins α-actinin, γ-filamin, and telethonin. In addition, we show that calsarcins interact with the PDZ-LIM domain protein ZASP/Cypher/Oracle, which also localizes to the Z-disc. Calsarcins represent a novel family of sarcomeric proteins that serve as focal points for the interactions of an array of proteins involved in Z-disc structure and signal transduction in striated muscle.",
author = "Norbert Frey and Olson, {Eric N.}",
year = "2002",
month = "4",
day = "19",
doi = "10.1074/jbc.M200712200",
language = "English (US)",
volume = "277",
pages = "13998--14004",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "16",

}

TY - JOUR

T1 - Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins

AU - Frey, Norbert

AU - Olson, Eric N.

PY - 2002/4/19

Y1 - 2002/4/19

N2 - The Z-disc is a highly specialized multiprotein complex of striated muscles that serves as the interface of the sarcomere and the cytoskeleton. In addition to its role in muscle contraction, its juxtaposition to the plasma membrane suggests additional functions of the Z-disc in sensing and transmitting external and internal signals. Recently, we described two novel striated muscle-specific proteins, calsarcin-1 and calsarcin-2, that bind α-actinin on the Z-disc and serve as intracellular binding proteins for calcineurin, a calcium/calmodulindependent phosphatase shown to be integral in cardiac hypertrophy as well as skeletal muscle differentiation and fiber-type specification. Here, we describe an additional member of the calsarcin family, calsarcin-3, which is expressed specifically in skeletal muscle and is enriched in fast-twitch muscle fibers. Like calsarcin-1 and calsarcin-2, calsarcin-3 interacts with calcineurin, and the Z-disc proteins α-actinin, γ-filamin, and telethonin. In addition, we show that calsarcins interact with the PDZ-LIM domain protein ZASP/Cypher/Oracle, which also localizes to the Z-disc. Calsarcins represent a novel family of sarcomeric proteins that serve as focal points for the interactions of an array of proteins involved in Z-disc structure and signal transduction in striated muscle.

AB - The Z-disc is a highly specialized multiprotein complex of striated muscles that serves as the interface of the sarcomere and the cytoskeleton. In addition to its role in muscle contraction, its juxtaposition to the plasma membrane suggests additional functions of the Z-disc in sensing and transmitting external and internal signals. Recently, we described two novel striated muscle-specific proteins, calsarcin-1 and calsarcin-2, that bind α-actinin on the Z-disc and serve as intracellular binding proteins for calcineurin, a calcium/calmodulindependent phosphatase shown to be integral in cardiac hypertrophy as well as skeletal muscle differentiation and fiber-type specification. Here, we describe an additional member of the calsarcin family, calsarcin-3, which is expressed specifically in skeletal muscle and is enriched in fast-twitch muscle fibers. Like calsarcin-1 and calsarcin-2, calsarcin-3 interacts with calcineurin, and the Z-disc proteins α-actinin, γ-filamin, and telethonin. In addition, we show that calsarcins interact with the PDZ-LIM domain protein ZASP/Cypher/Oracle, which also localizes to the Z-disc. Calsarcins represent a novel family of sarcomeric proteins that serve as focal points for the interactions of an array of proteins involved in Z-disc structure and signal transduction in striated muscle.

UR - http://www.scopus.com/inward/record.url?scp=0037134462&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037134462&partnerID=8YFLogxK

U2 - 10.1074/jbc.M200712200

DO - 10.1074/jbc.M200712200

M3 - Article

C2 - 11842093

AN - SCOPUS:0037134462

VL - 277

SP - 13998

EP - 14004

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 16

ER -