The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization (Q28247638)

Diaphanous related formin 2

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

8

Alfred Wittinghofer

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Atsushi Shimada

object named as

Atsushi Shimada

1

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Michael A. Geeves

object named as

Michael A Geeves

7

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Miklos Nyitrai

object named as

Miklós Nyitrai

2

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author name string

Ingrid R Vetter

3

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Dorothee Kühlmann

4

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Beáta Bugyi

5

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Shuh Narumiya

Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain

6

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language of work or name

English

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publication date

27 February 2004

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published in

Molecular Cell

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volume

13

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issue

4

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page(s)

511-22

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The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization

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The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition

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Mutant actins demonstrate a role for unpolymerized actin in control of transcription by serum response factor

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Role of formins in actin assembly: nucleation and barbed-end association

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Yeast formins regulate cell polarity by controlling the assembly of actin cables.

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Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation

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