Article (Scientific journals)
The Ras/Rap GTPase activating protein RASA3 : from gene structure to in vivo functions
Schurmans, Stéphane; Polizzi, Séléna; Scoumanne, Ariane et al.
2015In Advances in Biological Regulation, 57, p. 153-161
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Keywords :
Rasa3; GTPase activating protein; Megakaryocyte
Abstract :
[en] RASA3 (or GTPase Activating Protein III, R-Ras GTPase-activating protein, GAP1IP4BP) is a GTPase activating protein of the GAP1 subfamily which targets Ras and Rap1. RASA3 was originally purified from pig platelet membranes through its intrinsic ability to bind inositol 1,3,4,5-tetrakisphosphate (I(1,3,4,5)P4) with high affinity, hence its first name GAP1IP4BP (for GAP1 subfamily member which binds I(1,3,4,5)P4). RASA3 was thus the first I(1,3,4,5)P4 receptor identified and cloned. The in vitro and in vivo functions of RASA3 remained somewhat elusive for a long time. However, recently, using genetically-modified mice and cells derived from these mice, the function of RASA3 during megakaryopoiesis, megakaryocyte adhesion and migration as well as integrin signaling has been reported. The goal of this review is thus to summarize and comment recent and less recent data in the literature on RASA3, in particular on the in vivo function of this specific GAP1 subfamily member.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Schurmans, Stéphane  ;  Université de Liège - ULiège > Département de sciences fonctionnelles (DSF) > Biochimie métabolique vétérinaire
Polizzi, Séléna
Scoumanne, Ariane ;  Université de Liège - ULiège > GIGA-R : Labo de génétique fonctionnelle
Sayyed, Sufyan Ali ;  Université de Liège - ULiège > GIGA-R : Labo de génétique fonctionnelle
Molina Ortiz, Patricia ;  Université de Liège - ULiège > GIGA-R : Labo de génétique fonctionnelle
Language :
English
Title :
The Ras/Rap GTPase activating protein RASA3 : from gene structure to in vivo functions
Publication date :
2015
Journal title :
Advances in Biological Regulation
ISSN :
2212-4926
eISSN :
2212-4934
Publisher :
Elsevier
Volume :
57
Pages :
153-161
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 05 April 2015

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