ARAP1 regulates the ring size of circular dorsal ruffles through Arf1 and Arf5.

Molecular Biology of the Cell
Junya HasegawaToshiki Itoh

Abstract

Small guanosine triphosphatase (GTPase) ADP-ribosylation factors (Arfs) regulate membrane traffic and actin reorganization under the strict control of GTPase-activating proteins (GAPs). ARAP1 (Arf GAP with Rho GAP domain, ankyrin repeat, and PH domain 1) is an Arf GAP molecule with multiple PH domains that recognize phosphatidylinositol 3,4,5-trisphosphate. We found that growth factor stimulation induced localization of ARAP1 to an area of the plasma membrane inside the ring structure of circular dorsal ruffles (CDRs). Moreover, expression of ARAP1 increased the size of the CDR filamentous-actin ring in an Arf GAP activity-dependent manner, whereas smaller CDRs were formed by ARAP1 knockdown. In addition, expression of a dominant-negative mutant of Arf1 and Arf5, the substrates of ARAP1, expanded the size of CDRs, suggesting that the two Arf isoforms regulate ring structure downstream of ARAP1. Therefore our results reveal a novel molecular mechanism of CDR ring size control through the ARAP1-Arf1/5 pathway.

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Citations

Sep 3, 2013·Histochemistry and Cell Biology·Carmen ValenteDaniela Corda
Jan 9, 2013·The Journal of Biological Chemistry·Pei-Wen ChenPaul A Randazzo
Nov 24, 2012·Journal of Biochemistry·Toshiki Itoh, Junya Hasegawa
Nov 27, 2015·Journal of Immunology Research·Jouda GamaraSylvain G Bourgoin
Sep 3, 2016·Small GTPases·Cristina CasalouDuarte C Barral
May 5, 2017·Molecular Biology of the Cell·Alejandra ValdiviaRafael Garcia-Mata
Oct 8, 2014·Physiological Reviews·Shiro SuetsuguTadaomi Takenawa
Jan 24, 2019·International Journal of Molecular Sciences·Christine E TannaPei-Wen Chen
Jun 23, 2021·Archives of Biochemistry and Biophysics·Xiang QinYiyao Liu

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Methods Mentioned

BETA
GTPases
nucleotide exchange
transfection
PCR

Software Mentioned

FluoView
Photoshop

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