Valosin-containing protein (VCP) is a novel IQ motif-containing GTPase activating protein 1 (IQGAP1)-interacting protein

2017 ◽  
Vol 493 (4) ◽  
pp. 1384-1389
Author(s):  
Norimichi Itoh ◽  
Taku Nagai ◽  
Takashi Watanabe ◽  
Kentaro Taki ◽  
Toshitaka Nabeshima ◽  
...  
2009 ◽  
Vol 3 (3) ◽  
pp. 307-321 ◽  
Author(s):  
Fariba Kalantari ◽  
Patrick Auguste ◽  
Tahereh Ziafazeli ◽  
George Tzimas ◽  
Lars Malmström ◽  
...  

PLoS ONE ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. e0129314 ◽  
Author(s):  
Amr M. Ghaleb ◽  
Agnieszka B. Bialkowska ◽  
Ashley J. Snider ◽  
Dmitri V. Gnatenko ◽  
Yusuf A. Hannun ◽  
...  

2002 ◽  
Vol 22 (24) ◽  
pp. 8721-8734 ◽  
Author(s):  
Takeshi Nakamura ◽  
Misako Komiya ◽  
Kiyoaki Sone ◽  
Eiji Hirose ◽  
Noriko Gotoh ◽  
...  

ABSTRACT Neurotrophins are key regulators of the fate and shape of neuronal cells and act as guidance cues for growth cones by remodeling the actin cytoskeleton. Actin dynamics is controlled by Rho GTPases. We identified a novel Rho GTPase-activating protein (Grit) for Rho/Rac/Cdc42 small GTPases. Grit was abundant in neuronal cells and directly interacted with TrkA, a high-affinity receptor for nerve growth factor (NGF). Another pool of Grit was recruited to the activated receptor tyrosine kinase through its binding to N-Shc and CrkL/Crk, adapter molecules downstream of activated receptor tyrosine kinases. Overexpression of the TrkA-binding region of Grit inhibited NGF-induced neurite elongation. Further, we found some tendency for neurite promotion in full-length Grit-overexpressing PC12 cells upon NGF stimulation. These results suggest that Grit, a novel TrkA-interacting protein, regulates neurite outgrowth by modulating the Rho family of small GTPases.


2005 ◽  
Vol 69 (4) ◽  
pp. 861-865 ◽  
Author(s):  
Fumitaka ICHIOKA ◽  
Mio HORII ◽  
Keiichi KATOH ◽  
Yoshinori TERASAWA ◽  
Hideki SHIBATA ◽  
...  

2019 ◽  
Author(s):  
Makoto Tanaka ◽  
Tomohiro Osanai ◽  
Yoshimi Homma ◽  
Kenji Hanada ◽  
Ken Okumura ◽  
...  

AbstractPhospholipase C (PLC)-δ1, activated by p122RhoGTPase-activating protein (GAP)/deleted in liver cancer-1 (p122RhoGAP/DLC-1), contributes to the coronary spastic angina (CSA) pathogenesis. The present study aims to further investigate the p122RhoGAP/DLC-1 protein. We examined molecules assisting this protein and identified a scaffold protein—IQ motif-containing GTPase-activating protein 1 (IQGAP1). IQGAP1-C binds to the steroidogenic acute regulatory-related lipid transfer (START) domain of p122RhoGAP/DLC-1, and PLC-δ1 binds to IQGAP1-N, forming a complex. In fluorescence microscopy, small dots of PLC-δ1 created fine linear arrays like microtubules, and IQGAP1 and p122RhoGAP/DLC-1 were colocated in the cytoplasm with PLC-δ1. Ionomycin induced the raft recruitment of the PLC-δ1, IQGAP1, and p122RhoGAP/DLC-1 complex by translocation to the plasma membrane (PM), indicating the movement of this complex is along microtubules with the motor protein kinesin. Moreover, the IQGAP1 protein was elevated in skin fibroblasts obtained from patients with CSA, and it enhanced the PLC activity and peak intracellular calcium concentration in response to acetylcholine. IQGAP1, a novel stimulating protein, forms a complex with p122RhoGAP/DLC-1 and PLC-δ1 that moves along microtubules and enhances the PLC activity.


Sign in / Sign up

Export Citation Format

Share Document