Redefining actin dynamics of the pointed-end complex in striated muscle

Jessika Iwanski; Carol C. Gregorio; Mert Colpan

doi:10.1016/j.tcb.2021.06.006

Redefining actin dynamics of the pointed-end complex in striated muscle

Jessika Iwanski
, Carol C. Gregorio
, Mert Colpan

Research output: Contribution to journal › Short survey › peer-review

7 Scopus citations

Abstract

Striated muscle is intricately designed to provide efficient and powerful muscle contractions. Recently, a long sought-after missing component of the thin filament pointed-end machinery was discovered: cyclase-associated protein 2 (CAP2). CAP2 was identified as a crucial contributor to actin polymerization, striated muscle development, and severe muscle disease when mutated.

Original language	English (US)
Pages (from-to)	708-711
Number of pages	4
Journal	Trends in Cell Biology
Volume	31
Issue number	9
DOIs	https://doi.org/10.1016/j.tcb.2021.06.006
State	Published - Sep 2021

Keywords

actin
muscle
myopathy
sarcomere
thin filament

ASJC Scopus subject areas

Cell Biology

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10.1016/j.tcb.2021.06.006

Cite this

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title = "Redefining actin dynamics of the pointed-end complex in striated muscle",

abstract = "Striated muscle is intricately designed to provide efficient and powerful muscle contractions. Recently, a long sought-after missing component of the thin filament pointed-end machinery was discovered: cyclase-associated protein 2 (CAP2). CAP2 was identified as a crucial contributor to actin polymerization, striated muscle development, and severe muscle disease when mutated.",

keywords = "actin, muscle, myopathy, sarcomere, thin filament",

author = "Jessika Iwanski and Gregorio, \{Carol C.\} and Mert Colpan",

note = "Funding Information: This work was supported by the University of Arizona Sarver Heart Center Marjorie Hornbeck Memorial Research Grant and the American Heart Association Postdoctoral Fellowship 19POST34450023 (to M.C.), the National Heart, Lung, and Blood Institute of the National Institutes of Health grants F30HL151139 and T32HL007249 (to J.I.), and R01HL123078 (to C.C.G.). The authors thank all members of the laboratory for extensive discussions and Dr Velia Fowler for being the founder in the field of pointed-end actin-binding proteins. Publisher Copyright: {\textcopyright} 2021 Elsevier Ltd",

year = "2021",

month = sep,

doi = "10.1016/j.tcb.2021.06.006",

language = "English (US)",

volume = "31",

pages = "708--711",

journal = "Trends in Cell Biology",

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}

TY - JOUR

T1 - Redefining actin dynamics of the pointed-end complex in striated muscle

AU - Iwanski, Jessika

AU - Gregorio, Carol C.

AU - Colpan, Mert

N1 - Funding Information: This work was supported by the University of Arizona Sarver Heart Center Marjorie Hornbeck Memorial Research Grant and the American Heart Association Postdoctoral Fellowship 19POST34450023 (to M.C.), the National Heart, Lung, and Blood Institute of the National Institutes of Health grants F30HL151139 and T32HL007249 (to J.I.), and R01HL123078 (to C.C.G.). The authors thank all members of the laboratory for extensive discussions and Dr Velia Fowler for being the founder in the field of pointed-end actin-binding proteins. Publisher Copyright: © 2021 Elsevier Ltd

PY - 2021/9

Y1 - 2021/9

N2 - Striated muscle is intricately designed to provide efficient and powerful muscle contractions. Recently, a long sought-after missing component of the thin filament pointed-end machinery was discovered: cyclase-associated protein 2 (CAP2). CAP2 was identified as a crucial contributor to actin polymerization, striated muscle development, and severe muscle disease when mutated.

AB - Striated muscle is intricately designed to provide efficient and powerful muscle contractions. Recently, a long sought-after missing component of the thin filament pointed-end machinery was discovered: cyclase-associated protein 2 (CAP2). CAP2 was identified as a crucial contributor to actin polymerization, striated muscle development, and severe muscle disease when mutated.

KW - actin

KW - muscle

KW - myopathy

KW - sarcomere

KW - thin filament

UR - https://www.scopus.com/pages/publications/85110389973

UR - https://www.scopus.com/pages/publications/85110389973#tab=citedBy

U2 - 10.1016/j.tcb.2021.06.006

DO - 10.1016/j.tcb.2021.06.006

M3 - Short survey

C2 - 34266732

AN - SCOPUS:85110389973

SN - 0962-8924

VL - 31

SP - 708

EP - 711

JO - Trends in Cell Biology

JF - Trends in Cell Biology

IS - 9

ER -

Redefining actin dynamics of the pointed-end complex in striated muscle

Abstract

Keywords

ASJC Scopus subject areas

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