Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility (Q24682432)

2

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N Kinoshita

3

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Y Kawano

4

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Y Matsuoka

5

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V Bennett

6

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Y Matsuura

7

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K Kaibuchi

Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons

8

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language of work or name

English

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publication date

19 April 1999

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published in

Journal of Cell Biology

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volume

145

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page(s)

347-61

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issue

2

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cites work

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Modulation of spectrin-actin assembly by erythrocyte adducin

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho

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Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase

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p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions

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30 May 2018

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30 May 2018

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Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation

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Phosphorylation of moesin by rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures

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Involvement of rho p21 in the GTP-enhanced calcium ion sensitivity of smooth muscle contraction

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p160 RhoA-binding kinase ROKalpha induces neurite retraction

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Mapping the domain structure of human erythrocyte adducin

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Spectrin in the leading lamella of cultured chicken fibroblasts

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Identifiers

DOI

10.1083/JCB.145.2.347

1 reference

4883546

4883546

1 reference

1 reference

1 reference