Domain analysis of alpha-actinin reveals new aspects of its association with F-actin during cytokinesis. (Q50559954)

15 March 2018

title

Domain analysis of alpha-actinin reveals new aspects of its association with F-actin during cytokinesis. (English)

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15 March 2018

author name string

Shyan Huey Low

1

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15 March 2018

Svetlana Mukhina

2

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15 March 2018

Vinayaka Srinivas

3

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15 March 2018

Chang Zhi Ng

4

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15 March 2018

Maki Murata-Hori

5

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15 March 2018

language of work or name

English

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publication date

15 March 2010

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15 March 2018

Experimental Cell Research

published in

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15 March 2018

volume

316

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15 March 2018

issue

12

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15 March 2018

page(s)

1925-1934

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15 March 2018

Alpha-actinin is required for tightly regulated remodeling of the actin cortical network during cytokinesis

cites work

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Interchain binding at the tail end of the Drosophila spectrin molecule

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Calcium-sensitive non-muscle alpha-actinin contains EF-hand structures and highly conserved regions

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An interaction between alpha-actinin and the beta 1 integrin subunit in vitro

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An interaction between zyxin and alpha-actinin

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Characterization of palladin, a novel protein localized to stress fibers and cell adhesions

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Characterization of human palladin, a microfilament-associated protein

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Distinct roles of the equatorial and polar cortices in the cleavage of adherent cells

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Cortical actin turnover during cytokinesis requires myosin II.

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Putting the brakes on cytokinesis with alpha-actinin.

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The cytoskeletal/non-muscle isoform of alpha-actinin is phosphorylated on its actin-binding domain by the focal adhesion kinase

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The three-dimensional structure of alpha-actinin obtained by cryoelectron microscopy suggests a model for Ca(2+)-dependent actin binding.

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PIP2 hydrolysis and calcium release are required for cytokinesis in Drosophila spermatocytes.

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Human skeletal muscle-specific alpha-actinin-2 and -3 isoforms form homodimers and heterodimers in vitro and in vivo

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Identifiers

DOI

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15 March 2018

PubMed ID

20230817

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15 March 2018