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Ribosomal S6 kinase (RSK) phosphorylates filamin A on an important regulatory site :Implications for RSK in the control of cell migration

Record Type:	Electronic resources : Monograph/item
Title/Author:	Ribosomal S6 kinase (RSK) phosphorylates filamin A on an important regulatory site :
Reminder of title:	Implications for RSK in the control of cell migration
Author:	Woo, Michele Sue-Ann.
Description:	149 p.
Notes:	Adviser: John Blenis.
Notes:	Source: Dissertation Abstracts International, Volume: 65-05, Section: B, page: 2193.
Contained By:	Dissertation Abstracts International65-05B.
Subject:	Biology, Cell.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3132030
ISBN:	0496792709

Ribosomal S6 kinase (RSK) phosphorylates filamin A on an important regulatory site :Implications for RSK in the control of cell migration
Woo, Michele Sue-Ann.

Ribosomal S6 kinase (RSK) phosphorylates filamin A on an important regulatory site :Implications for RSK in the control of cell migration [electronic resource] - 149 p.

Adviser: John Blenis.

Thesis (Ph.D.)--Harvard University, 2004.

The goal of this thesis is to characterize the cytoskeletal protein filamin A (FLNa) as a novel RSK target. We show that the amino-terminal kinase domain of RSK phosphorylates FLNa on serine 2152 (Ser2152) in response to mitogens. Inhibition of mitogen-activated protein kinase (MAPK) signaling or mutation of Ser2152 to alanine on FLNa prevents epidermal growth factor (EGF)-stimulated phosphorylation of FLNa in vivo. Furthermore, expression of wild-type RSK greatly enhances FLNa Ser2152 phosphorylation, whereas expression of kinase-inactive RSK or down-regulation of endogenous RSK antagonizes this phosphorylation. Strikingly, EGF-induced, FLNa-dependent migration of human melanoma cells requires activation of the MAPK pathway. Together, these data provide substantial evidence that RSK phosphorylates FLNa on Ser2152 in vivo. Given that phosphorylation of FLNa on Ser2152 is required for p21-activated kinase-1 (Pak1)-mediated membrane ruffling, our results suggest that RSK may play a role in the control of actin cytoskeletal dynamics.

ISBN: 0496792709Subjects--Topical Terms:

226967
Biology, Cell.

Ribosomal S6 kinase (RSK) phosphorylates filamin A on an important regulatory site :Implications for RSK in the control of cell migration
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500 $a Source: Dissertation Abstracts International, Volume: 65-05, Section: B, page: 2193.
502 $a Thesis (Ph.D.)--Harvard University, 2004.
520 # $a The goal of this thesis is to characterize the cytoskeletal protein filamin A (FLNa) as a novel RSK target. We show that the amino-terminal kinase domain of RSK phosphorylates FLNa on serine 2152 (Ser2152) in response to mitogens. Inhibition of mitogen-activated protein kinase (MAPK) signaling or mutation of Ser2152 to alanine on FLNa prevents epidermal growth factor (EGF)-stimulated phosphorylation of FLNa in vivo. Furthermore, expression of wild-type RSK greatly enhances FLNa Ser2152 phosphorylation, whereas expression of kinase-inactive RSK or down-regulation of endogenous RSK antagonizes this phosphorylation. Strikingly, EGF-induced, FLNa-dependent migration of human melanoma cells requires activation of the MAPK pathway. Together, these data provide substantial evidence that RSK phosphorylates FLNa on Ser2152 in vivo. Given that phosphorylation of FLNa on Ser2152 is required for p21-activated kinase-1 (Pak1)-mediated membrane ruffling, our results suggest that RSK may play a role in the control of actin cytoskeletal dynamics.
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