Results 21 to 30 of about 25,588 (204)

Rabaptin5 is recruited to endosomes by Rab4 and Rabex5 to regulate endosome maturation [PDF]

open access: yes, 2015
Rab GTPases control membrane identity, fusion, and transport by interaction with effector proteins. Effectors that influence the activation/inactivation cycle of their own or other Rabs contribute to the timely conversion of Rab identities.
Buser, Dominik P.   +3 more
core   +1 more source

The plant-pathogen haustorial interface at a glance [PDF]

open access: yes, 2020
Many filamentous pathogens invade plant cells through specialized hyphae called haustoria. These infection structures are enveloped by a newly synthesized plant-derived membrane called the extrahaustorial membrane (EHM).
Bozkurt, Tolga O., Kamoun, Sophien
core   +1 more source

Coordination of the Rab5 Cycle on Macropinosomes [PDF]

open access: yesTraffic, 2011
The GTPase Rab5a regulates the homotypic and heterotypic fusion of membranous organelles during the early stages of endocytosis. Many of the molecules which regulate the Rab5a cycle of association with membranes, activation, deactivation and dissociation are known.
Feliciano, William David   +3 more
openaire   +3 more sources

Integration of two RAB5 groups during endosomal transport in plants

open access: yeseLife, 2018
RAB5 is a key regulator of endosomal functions in eukaryotic cells. Plants possess two different RAB5 groups, canonical and plant-unique types, which act via unknown counteracting mechanisms.
Emi Ito   +6 more
doaj   +1 more source

Specific Rab GTPase-activating proteins define the Shiga toxin and epidermal growth factor uptake pathways [PDF]

open access: yes, 2007
Rab family guanosine triphosphatases (GTPases) together with their regulators define specific pathways of membrane traffic within eukaryotic cells. In this study, we have investigated which Rab GTPase-activating proteins (GAPs) can interfere with the ...
Barr, Francis A.   +5 more
core   +2 more sources

Effect of EGF-Receptor Tyrosine Kinase Inhibitor on Rab5 Function During Endocytosis [PDF]

open access: yes, 2012
Tyrosine autophosphorylation within the cytoplasmic tail of EGF-receptor is a key event, which in turn recruits several factors including Shc, Grb2 and Rin1 that are essential activities for receptor-mediated endocytosis and signaling.
Barbieri, M. Alejandro   +2 more
core   +2 more sources

CMTM7 as a novel molecule of ATG14L-Beclin1-VPS34 complex enhances autophagy by Rab5 to regulate tumorigenicity

open access: yesCell Communication and Signaling, 2021
Background CMTM7 is a tumor suppressor that positively regulates EGFR degradation by promoting Rab5 activation, and plays a vital role in tumor progression. Rab5 forms complexes with Beclin1 and VPS34, and acts in the early stage of autophagy.
Baocai Liu   +7 more
doaj   +1 more source

Rab5 GTPases are required for optimal TORC2 function [PDF]

open access: yesJournal of Cell Biology, 2018
Target of rapamycin complex-2 (TORC2), a conserved protein kinase complex, is an indispensable regulator of plasma membrane homeostasis. In budding yeast (Saccharomyces cerevisiae), the essential downstream effector of TORC2 is protein kinase Ypk1 and its paralog Ypk2.
Melissa N. Locke, Jeremy Thorner
openaire   +4 more sources

Abnormal α-synuclein interactions with rab3a and rabphilin in diffuse Lewy body disease

open access: yesNeurobiology of Disease, 2004
The present study examines α-synuclein interactions with rab3a and rabphilin by antibody arrays, immunoprecipitation and pull-down methods in the entorhinal cortex of control cases and in diffuse Lewy body disease (LBD) cases.
E Dalfó   +4 more
doaj   +1 more source

Rab GTPase Mediating Regulation of NALP3 in Colorectal Cancer

open access: yesMolecules, 2020
The NALP3 inflammasome signaling contributes to inflammation within tumor tissues. This inflammation may be promoted by the vesicle trafficking of inflammasome components and cytokines. Rab5, Rab7 and Rab11 regulate vesicle trafficking. However, the role
Gülçin Tezcan   +5 more
doaj   +1 more source

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