The GDI-like solubilizing factor PDEδ sustains the spatial organization and signalling of Ras family proteins

2011 ◽  
Vol 14 (2) ◽  
pp. 148-158 ◽  
Author(s):  
Anchal Chandra ◽  
Hernán E. Grecco ◽  
Venkat Pisupati ◽  
David Perera ◽  
Liam Cassidy ◽  
...  
Keyword(s):  
Spatial Organization ◽  
Ras Family ◽  
Ras Family Proteins

scholarly journals Erratum: The GDI-like solubilizing factor PDEδ sustains the spatial organization and signalling of Ras family proteins

2012 ◽  
Vol 14 (3) ◽  
pp. 329-329 ◽  
Author(s):  
Anchal Chandra ◽  
Hernán E. Grecco ◽  
Venkat Pisupati ◽  
David Perera ◽  
Liam Cassidy ◽  
...  
Keyword(s):  
Spatial Organization ◽  
Ras Family ◽  
Ras Family Proteins

Mammalian expression vectors for Ras family proteins: Generation and use of expression constructs to analyze Ras family function

2001 ◽  
pp. 3-36 ◽  
Author(s):  
James J. Fiordalisi ◽  
Ronald L. Johnson ◽  
Aylin S. Ülkü ◽  
Channing J. Der ◽  
Adrienne D. Cox
Keyword(s):  
Expression Vectors ◽  
Family Function ◽  
Mammalian Expression ◽  
Ras Family ◽  
Ras Family Proteins

Structural fingerprints, interactions, and signaling networks of RAS family proteins beyond RAS isoforms

2018 ◽  
Vol 53 (2) ◽  
pp. 130-156 ◽  
Author(s):  
Saeideh Nakhaei-Rad ◽  
Fereshteh Haghighi ◽  
Parivash Nouri ◽  
Soheila Rezaei Adariani ◽  
Jana Lissy ◽  
...  
Keyword(s):  
Signaling Networks ◽  
Ras Family ◽  
Ras Isoforms ◽  
Ras Family Proteins

Ras family proteins: New players involved in the diplotene arrest of Xenopus oocytes

1998 ◽  
Vol 90 (8) ◽  
pp. 573-583 ◽  
Author(s):  
Catherine Jessus ◽  
Hélène Rime ◽  
René Ozon
Keyword(s):  
Xenopus Oocytes ◽  
Ras Family ◽  
Ras Family Proteins

Proteomic analysis reveals that pheophorbide a-mediated photodynamic treatment inhibits prostate cancer growth by hampering GDP-GTP exchange of ras-family proteins

2018 ◽  
Vol 23 ◽  
pp. 35-39 ◽  
Author(s):  
Dan Dan Xu ◽  
Chong Bing Xu ◽  
Hon Ming Lam ◽  
Fuk-Ling Wong ◽  
Albert Wing Nang Leung ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Proteomic Analysis ◽  
Cancer Growth ◽  
Pheophorbide A ◽  
Photodynamic Treatment ◽  
Ras Family ◽  
Ras Family Proteins

scholarly journals Statin-Induced Cancer Cell Death Can Be Mechanistically Uncoupled from Prenylation of RAS Family Proteins

2017 ◽  
Vol 78 (5) ◽  
pp. 1347-1357 ◽  
Author(s):  
Rosemary Yu ◽  
Joseph Longo ◽  
Jenna E. van Leeuwen ◽  
Peter J. Mullen ◽  
Wail Ba-Alawi ◽  
...  
Keyword(s):  
Cell Death ◽  
Cancer Cell ◽  
Cancer Cell Death ◽  
Ras Family ◽  
Ras Family Proteins

scholarly journals The polarity of myxobacterial gliding is regulated by direct interactions between the gliding motors and the Ras homolog MglA

2014 ◽  
Vol 112 (2) ◽  
pp. E186-E193 ◽  
Author(s):  
Beiyan Nan ◽  
Jigar N. Bandaria ◽  
Kathy Y. Guo ◽  
Xue Fan ◽  
Amirpasha Moghtaderi ◽  
...  
Keyword(s):  
Spatial Distribution ◽  
Cell Polarity ◽  
Myxococcus Xanthus ◽  
Proton Motive Force ◽  
Gliding Motility ◽  
Cellular Polarity ◽  
Gtpase Activating Protein ◽  
Chemosensory Pathway ◽  
Ras Family ◽  
Ras Family Proteins

Gliding motility in Myxococcus xanthus is powered by flagella stator homologs that move in helical trajectories using proton motive force. The Frz chemosensory pathway regulates the cell polarity axis through MglA, a Ras family GTPase; however, little is known about how MglA establishes the polarity of gliding, because the gliding motors move simultaneously in opposite directions. Here we examined the localization and dynamics of MglA and gliding motors in high spatial and time resolution. We determined that MglA localizes not only at the cell poles, but also along the cell bodies, forming a decreasing concentration gradient toward the lagging cell pole. MglA directly interacts with the motor protein AglR, and the spatial distribution of AglR reversals is positively correlated with the MglA gradient. Thus, the motors moving toward lagging cell poles are less likely to reverse, generating stronger forward propulsion. MglB, the GTPase-activating protein of MglA, regulates motor reversal by maintaining the MglA gradient. Our results suggest a mechanism whereby bacteria use Ras family proteins to modulate cellular polarity.

Sign in / Sign up

Export Citation Format

Share Document