Molecular determinants of calpain-dependent cleavage of junctophilin-2 protein in cardiomyocytes

Ang Guo; Duane Hall; Caimei Zhang; Tianqing Peng; Jordan D. Miller; William Kutschke; Chad E. Grueter; Frances L. Johnson; Richard Z. Lin; Long Sheng Song

doi:10.1074/jbc.M115.652396

Molecular determinants of calpain-dependent cleavage of junctophilin-2 protein in cardiomyocytes

Ang Guo
, Duane Hall
, Caimei Zhang
, Tianqing Peng
, Jordan D. Miller
, William Kutschke
, Chad E. Grueter
, Frances L. Johnson
, Richard Z. Lin
, Long Sheng Song

Physiology and Biophysics

University of Iowa
Western University
Mayo Clinic Rochester, MN

Research output: Contribution to journal › Article › peer-review

68 Scopus citations

Abstract

Background: Down-regulation of junctophilin-2 is associated with a variety of cardiac diseases. Results: Junctophilin-2 is cleaved by calpain at multiple sites, resulting in dysfunctional junctophilin-2 truncations. Conclusion: Calpain-mediated proteolysis contributes to posttranslational down-regulation of junctophilin-2. Significance: These data reveal, for the first time, the detailed molecular determinants responsible for calpain proteolysis of junctophilin-2.

Original language	English
Pages (from-to)	17946-17955
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	290
Issue number	29
DOIs	https://doi.org/10.1074/jbc.M115.652396
State	Published - Jul 17 2015

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title = "Molecular determinants of calpain-dependent cleavage of junctophilin-2 protein in cardiomyocytes",

abstract = "Background: Down-regulation of junctophilin-2 is associated with a variety of cardiac diseases. Results: Junctophilin-2 is cleaved by calpain at multiple sites, resulting in dysfunctional junctophilin-2 truncations. Conclusion: Calpain-mediated proteolysis contributes to posttranslational down-regulation of junctophilin-2. Significance: These data reveal, for the first time, the detailed molecular determinants responsible for calpain proteolysis of junctophilin-2.",

author = "Ang Guo and Duane Hall and Caimei Zhang and Tianqing Peng and Miller, \{Jordan D.\} and William Kutschke and Grueter, \{Chad E.\} and Johnson, \{Frances L.\} and Lin, \{Richard Z.\} and Song, \{Long Sheng\}",

note = "Publisher Copyright: {\textcopyright} 2015 by The American Society for Biochemistry and Molecular Biology, Inc.",

year = "2015",

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doi = "10.1074/jbc.M115.652396",

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T1 - Molecular determinants of calpain-dependent cleavage of junctophilin-2 protein in cardiomyocytes

AU - Guo, Ang

AU - Hall, Duane

AU - Zhang, Caimei

AU - Peng, Tianqing

AU - Miller, Jordan D.

AU - Kutschke, William

AU - Grueter, Chad E.

AU - Johnson, Frances L.

AU - Lin, Richard Z.

AU - Song, Long Sheng

PY - 2015/7/17

Y1 - 2015/7/17

N2 - Background: Down-regulation of junctophilin-2 is associated with a variety of cardiac diseases. Results: Junctophilin-2 is cleaved by calpain at multiple sites, resulting in dysfunctional junctophilin-2 truncations. Conclusion: Calpain-mediated proteolysis contributes to posttranslational down-regulation of junctophilin-2. Significance: These data reveal, for the first time, the detailed molecular determinants responsible for calpain proteolysis of junctophilin-2.

AB - Background: Down-regulation of junctophilin-2 is associated with a variety of cardiac diseases. Results: Junctophilin-2 is cleaved by calpain at multiple sites, resulting in dysfunctional junctophilin-2 truncations. Conclusion: Calpain-mediated proteolysis contributes to posttranslational down-regulation of junctophilin-2. Significance: These data reveal, for the first time, the detailed molecular determinants responsible for calpain proteolysis of junctophilin-2.

UR - https://www.scopus.com/pages/publications/84937458779

U2 - 10.1074/jbc.M115.652396

DO - 10.1074/jbc.M115.652396

M3 - Article

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AN - SCOPUS:84937458779

SN - 0021-9258

VL - 290

SP - 17946

EP - 17955

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 29

ER -

Molecular determinants of calpain-dependent cleavage of junctophilin-2 protein in cardiomyocytes

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