Rab11 proteins in health and disease.

Biochem Soc Trans

Molecular Cell Biology Laboratory, Department of Biochemistry, BioSciences Institute, University College Cork, Cork, Ireland.

Published: December 2012

Comprising over 60 members, Rab proteins constitute the largest branch of the Ras superfamily of low-molecular-mass G-proteins. This protein family have been primarily implicated in various aspects of intracellular membrane trafficking processes. On the basis of distinct subfamily-specific sequence motifs, many Rabs have been grouped into subfamilies. The Rab11 GTPase subfamily comprises three members: Rab11a, Rab11b and Rab25/Rab11c, which, between them, have been demonstrated to bind more than 30 proteins. In the present paper, we review the function of the Rab11 subfamily. We describe their localization and primary functional roles within the cell and their implication, to date, in disease processes. We also summarize the protein machinery currently known to regulate or mediate their functions and the cargo molecules which they have been shown to transport.

Download full-text PDF

Source
http://dx.doi.org/10.1042/BST20120157DOI Listing

Publication Analysis

Top Keywords

rab11 proteins
4
proteins health
4
health disease
4
disease comprising
4
comprising members
4
members rab
4
rab proteins
4
proteins constitute
4
constitute largest
4
largest branch
4

Similar Publications

The TRAPP (TRAnsport Protein Particle) protein complex is a multi-subunit complex involved in vesicular transport between intracellular compartments. The TRAPP complex plays an important role in endoplasmic reticulum-to-Golgi and Golgi-to-plasma membrane transport, as well as autophagy. TRAPP complexes comprise a core complex, TRAPPI, and the association of peripheral protein subunits to make two complexes, known as TRAPPII and TRAPPIII, which act as Guanine Nucleotide Exchange Factors (GEFs) of Rab11 and Rab1, respectively.

View Article and Find Full Text PDF

The transmembrane protein Synapse Differentiation Induced Gene 4 (SynDIG4) functions as an auxiliary factor of AMPA receptors (AMPARs) and plays a critical role in excitatory synapse plasticity as well as hippocampal-dependent learning and memory. Mice lacking SynDIG4 have reduced surface expression of GluA1 and GluA2 and are impaired in single tetanus-induced long-term potentiation and NMDA receptor (NMDAR)-dependent long-term depression. These findings suggest that SynDIG4 may play an important role in regulating AMPAR distribution through intracellular trafficking mechanisms; however, the precise roles by which SynDIG4 governs AMPAR distribution remain unclear.

View Article and Find Full Text PDF

To inhibit endocytic entry of some viruses, cells promote acidification of endosomes by expressing the short isoform of human nuclear receptor 7 (NCOA7) which increases activity of vacuolar ATPase (V-ATPase). While we found that HIV-1 infection of primary T cells led to acidification of endosomes, NCOA7 levels were only marginally affected. Contrastingly, levels of the 50 kDa form of the sodium/hydrogen exchanger 6 (NHE6) were greatly reduced.

View Article and Find Full Text PDF

The potential role of vesicle transport-related small GTPases rabs in abiotic stress responses.

Plant Physiol Biochem

December 2024

Key Laboratory of Agricultural Biosafety and Green Production of Upper Yangtze River (Ministry of Education)/College of Horticulture and Landscape Architecture, Southwest University, Chongqing, 400715, China; State Cultivation Base of Crop Stress Biology for Southern Mountainous Land of Southwest University/Academy of Agricultural Sciences of Southwest University, Chongqing, 400715, China. Electronic address:

Rab GTPases are a class of small GTP-binding proteins, play crucial roles in the membrane transport machinery with in eukaryotic cells. They dynamically regulate the precise targeting and tethering of transport vesicles to specific compartments by transitioning between active and inactive states. In plants, Rab GTPases are classified into eight distinct subfamilies: Rab1/D, Rab2/B, Rab5/F, Rab6/H, Rab7/G, Rab8/E, Rab11/A, and Rab18/C.

View Article and Find Full Text PDF

TAT-1, a phosphatidylserine flippase, affects molting and regulates membrane trafficking in the epidermis of C. elegans.

Genetics

December 2024

Department of Molecular Biology, College of Agriculture, Life Sciences and Natural Resources, University of Wyoming, Laramie, Wyoming 82071.

Membrane trafficking is a conserved process required for import, export, movement, and distribution of proteins and other macromolecules within cells. The Caenorhabditis elegans NIMA-related kinases NEKL-2 (human NEK8/9) and NEKL-3 (human NEK6/7) are conserved regulators of membrane trafficking and are required for the completion of molting. Using a genetic approach we identified reduction-of-function mutations in tat-1 that suppress nekl-associated molting defects.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!