Results 81 to 90 of about 261,498 (196)

Dissecting the effects of GTPase and kinase domain mutations on LRRK2 endosomal localization and activity

Cell Reports, 2023
Summary: Parkinson’s disease-causing leucine-rich repeat kinase 2 (LRRK2) mutations lead to varying degrees of Rab GTPase hyperphosphorylation. Puzzlingly, LRRK2 GTPase-inactivating mutations—which do not affect intrinsic kinase activity—lead to higher ...
Capria Rinaldi, Christopher S. Waters, Zizheng Li, Karl Kumbier, Lee Rao, R. Jeremy Nichols, Matthew P. Jacobson, Lani F. Wu, Steven J. Altschuler   +8 more
doaj  

Overexpression of SYNGAP1 suppresses the proliferation of rectal adenocarcinoma via Wnt/β-Catenin signaling pathway

Discover Oncology
Rectal adenocarcinoma (READ) is a common malignant tumor of the digestive tract. Growing studies have confirmed Ras GTPase-activating proteins are involved in the progression of several tumors.
Yun Xiao, Ying Zhu, Jiaojiao Chen, Mei Wu, Lan Wang, Li Su, Fei Feng, Yanli Hou   +7 more
doaj   +1 more source

A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover

Nature Communications, 2017
The Parkinson’s disease‐associated LRRK2 protein is a multidomain Roco protein with GTPase activity. Here the authors use a multidisciplinary approach to characterize the GTPase mechanism of a homologous bacterial Roco protein and give mechanistic ...
Egon Deyaert, Lina Wauters, Giambattista Guaitoli, Albert Konijnenberg, Margaux Leemans, Susanne Terheyden, Arsen Petrovic, Rodrigo Gallardo, Laura M. Nederveen-Schippers, Panagiotis S. Athanasopoulos, Henderikus Pots, Peter J. M. Van Haastert, Frank Sobott, Christian Johannes Gloeckner, Rouslan Efremov, Arjan Kortholt, Wim Versées   +16 more
doaj   +1 more source

Modules in the photoreceptor RGS9-1•Gβ5L GTPase-accelerating protein complex control effector coupling, GTPase acceleration, protein folding, and stability [PDF]

, 2000
RGS (regulators of G protein signaling proteins regulate G protein signaling by accelerating GTP hydrolysis, but little is known about regulation of GTPase-accelerating protein (GAP) activities or roles of domains and subunits outside the catalytic cores.
Chen, Ching-Kang, El-Hodiri, Heithem M., He, Wei, Jamrich, Milan, Lu, Lisha, Simon, Melvin I., Slep, Kevin C., Wensel, Theodore G., Zhang, Xue   +8 more
core   +1 more source

The beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane. [PDF]

, 1995
The signal recognition particle receptor (SR) is required for the cotranslational targeting of both secretory and membrane proteins to the endoplasmic reticulum (ER) membrane.
Lauffer, L, Miller, JD, Tajima, S, Walter, P   +3 more
core  

Dissection of GTPase activating proteins reveals functional asymmetry in the COPI coat of budding yeast. [PDF]

, 2019
The Arf GTPase controls formation of the COPI vesicle coat. Recent structural models of COPI revealed the positioning of two Arf1 molecules in contrasting molecular environments.
Arakel, E., Estrada, A., Huranova, M., Rau, E., Schwappach, B., Spang, A.   +5 more
core   +1 more source

Kalirin12 interacts with dynamin

BMC Neuroscience, 2009
Background Guanine nucleotide exchange factors (GEFs) and their target Rho GTPases regulate cytoskeletal changes and membrane trafficking. Dynamin, a large force-generating GTPase, plays an essential role in membrane tubulation and fission in cells ...
Mains Richard E, Rabiner Chana A, Xin Xiaonan, Eipper Betty A   +3 more
doaj   +1 more source

Functional specialization of the yeast Rho1 GTP exchange factors [PDF]

, 2012
Rho GTPases are regulated in complex spatiotemporal patterns that may be dependent, in part at least, on the multiplicity of their GTP exchange factors (GEFs).
Cundell, M., Gray, J., Johnston, G., Krause, S., McGhie, J., Poon, P., Price, C.   +6 more
core  

Structural and mechanistic insights into regulation of the retromer coat by TBC1d5

Nature Communications, 2016
Retromer is recruited to endosomes by the small GTPase Rab7 and sorting nexin 3. Here, the authors report the interaction between a GTPase-activating protein TBC1d5 and Rab7, examine the biochemical details of the interaction with retromer, and discuss ...
Da Jia, Jin-San Zhang, Fang Li, Jing Wang, Zhihui Deng, Mark A. White, Douglas G. Osborne, Christine Phillips-Krawczak, Timothy S. Gomez, Haiying Li, Amika Singla, Ezra Burstein, Daniel D. Billadeau, Michael K. Rosen   +13 more
doaj   +1 more source

Inhibition by thiostrepton of the IF‐2‐dependent ribosomal GTPase [PDF]

, 1972
M. Grunberg‐Manago, J. Dondon, M. Graffe   +2 more
openalex   +1 more source