Implication of mouse Vps26b-Vps29-Vps35 retromer complex in sortilin trafficking. 2010

Ekyune Kim, and Youngjeon Lee, and Hyun-Ju Lee, and Ji Su Kim, and Bong-Seok Song, and Jae-Won Huh, and Sang-Rae Lee, and Sun-Uk Kim, and Sang-Hyun Kim, and Yonggeun Hong, and Insop Shim, and Kyu-Tae Chang
National Primate Research Center, Korea Research Institute of Bioscience and Biotechnology, 685-1 Yangcheong-ri, Ochang-eup, Chung-buk 363-883, Republic of Korea.

The retromer complex, which mediates retrograde transport from endosomes to the trans-Golgi network, is a heteropentameric complex that contains a multifunctional cargo recognition heterotrimer consisted of the vacuolar protein sorting (Vps) subunits Vps26, Vps29, and Vps35. In mammals, there are two different isoforms of Vps26, Vps26a and Vps26b, that localize to the endosome, and to the plasma membrane, respectively. To elucidate the biological significance of the Vps26b isoform, we generated Vps26b knockout mice and studied their molecular, histological, and behavioral phenotypes. We found that the loss of Vps26b results in no significant defects in the behavior, body size, and health of the mice. Vps26b-deficient mice showed a severe reduction of Vps35 protein at cellular level and lacked the Vps26b-Vps29-Vps35 retromer complex, despite the normal presence of the Vps26a-Vps29-Vps35 retromer complex. Relatively, the amount of sortilin was increased approximately 20% in the Vps26b-deficient mice, whereas the sorLA was normal. These results suggest that mouse Vps26b-Vps29-Vps35 retromer complex is implicated in the transport of sortilin from endosomes to the trans-Golgi network (TGN).

UI MeSH Term Description Entries
D011992 Endosomes Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface. Receptosomes,Endosome,Receptosome
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D051379 Mice The common name for the genus Mus. Mice, House,Mus,Mus musculus,Mice, Laboratory,Mouse,Mouse, House,Mouse, Laboratory,Mouse, Swiss,Mus domesticus,Mus musculus domesticus,Swiss Mice,House Mice,House Mouse,Laboratory Mice,Laboratory Mouse,Mice, Swiss,Swiss Mouse,domesticus, Mus musculus
D055503 Protein Multimerization The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS. Protein Dimerization,Protein Heteromultimerizaton,Protein Multimer Assembly,Protein Trimerization,Assembly, Protein Multimer,Dimerization, Protein,Heteromultimerizaton, Protein,Heteromultimerizatons, Protein,Multimer Assembly, Protein,Multimerization, Protein,Trimerization, Protein
D018345 Mice, Knockout Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes. Knockout Mice,Mice, Knock-out,Mouse, Knockout,Knock-out Mice,Knockout Mouse,Mice, Knock out
D021381 Protein Transport The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport. Cellular Protein Targeting,Gated Protein Transport,Protein Targeting, Cellular,Protein Translocation,Transmembrane Protein Transport,Vesicular Protein Transport,Protein Localization Processes, Cellular,Protein Sorting,Protein Trafficking,Protein Transport, Gated,Protein Transport, Transmembrane,Protein Transport, Vesicular,Traffickings, Protein
D021601 trans-Golgi Network A network of membrane compartments, located at the cytoplasmic side of the GOLGI APPARATUS, where proteins and lipids are sorted for transport to various locations in the cell or cell membrane. trans-Golgi Region,Network, trans-Golgi,Region, trans-Golgi,Regions, trans-Golgi,trans Golgi Network,trans Golgi Region,trans-Golgi Regions
D033921 Vesicular Transport Proteins A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported. Transport Proteins, Vesicular
D033942 Adaptor Proteins, Vesicular Transport A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found. Clathrin Adaptor,Clathrin Adaptor Protein Complex,Clathrin Assembly Protein,Clathrin Assembly Protein Complex,Clathrin Assembly Proteins,Clathrin-Associated Adaptor,Clathrin-Associated Protein,Vesicular Transport Adaptor Protein,Vesicular Transport Adaptor Protein Complex,Vesicular Transport Adaptor Proteins,Adaptor Protein Complexes, Vesicular Transport,Clathrin Adaptor Protein Complexes,Clathrin Adaptors,Clathrin Assembly Protein Complexes,Clathrin-Associated Adaptors,Clathrin-Associated Proteins,Vesicular Transport Adaptor Protein Complexes,Adaptor, Clathrin,Adaptor, Clathrin-Associated,Adaptors, Clathrin,Adaptors, Clathrin-Associated,Assembly Protein, Clathrin,Assembly Proteins, Clathrin,Clathrin Associated Adaptor,Clathrin Associated Adaptors,Clathrin Associated Protein,Clathrin Associated Proteins,Protein, Clathrin Assembly,Protein, Clathrin-Associated

Related Publications

Ekyune Kim, and Youngjeon Lee, and Hyun-Ju Lee, and Ji Su Kim, and Bong-Seok Song, and Jae-Won Huh, and Sang-Rae Lee, and Sun-Uk Kim, and Sang-Hyun Kim, and Yonggeun Hong, and Insop Shim, and Kyu-Tae Chang
June 2015, FEBS letters,
Ekyune Kim, and Youngjeon Lee, and Hyun-Ju Lee, and Ji Su Kim, and Bong-Seok Song, and Jae-Won Huh, and Sang-Rae Lee, and Sun-Uk Kim, and Sang-Hyun Kim, and Yonggeun Hong, and Insop Shim, and Kyu-Tae Chang
May 2024, Protein science : a publication of the Protein Society,
Ekyune Kim, and Youngjeon Lee, and Hyun-Ju Lee, and Ji Su Kim, and Bong-Seok Song, and Jae-Won Huh, and Sang-Rae Lee, and Sun-Uk Kim, and Sang-Hyun Kim, and Yonggeun Hong, and Insop Shim, and Kyu-Tae Chang
December 2012, The Plant cell,
Ekyune Kim, and Youngjeon Lee, and Hyun-Ju Lee, and Ji Su Kim, and Bong-Seok Song, and Jae-Won Huh, and Sang-Rae Lee, and Sun-Uk Kim, and Sang-Hyun Kim, and Yonggeun Hong, and Insop Shim, and Kyu-Tae Chang
January 2017, Journal of Parkinson's disease,
Ekyune Kim, and Youngjeon Lee, and Hyun-Ju Lee, and Ji Su Kim, and Bong-Seok Song, and Jae-Won Huh, and Sang-Rae Lee, and Sun-Uk Kim, and Sang-Hyun Kim, and Yonggeun Hong, and Insop Shim, and Kyu-Tae Chang
December 2024, Computational and structural biotechnology journal,
Ekyune Kim, and Youngjeon Lee, and Hyun-Ju Lee, and Ji Su Kim, and Bong-Seok Song, and Jae-Won Huh, and Sang-Rae Lee, and Sun-Uk Kim, and Sang-Hyun Kim, and Yonggeun Hong, and Insop Shim, and Kyu-Tae Chang
November 2005, Traffic (Copenhagen, Denmark),
Ekyune Kim, and Youngjeon Lee, and Hyun-Ju Lee, and Ji Su Kim, and Bong-Seok Song, and Jae-Won Huh, and Sang-Rae Lee, and Sun-Uk Kim, and Sang-Hyun Kim, and Yonggeun Hong, and Insop Shim, and Kyu-Tae Chang
March 2008, Traffic (Copenhagen, Denmark),
Ekyune Kim, and Youngjeon Lee, and Hyun-Ju Lee, and Ji Su Kim, and Bong-Seok Song, and Jae-Won Huh, and Sang-Rae Lee, and Sun-Uk Kim, and Sang-Hyun Kim, and Yonggeun Hong, and Insop Shim, and Kyu-Tae Chang
November 2017, Molecular microbiology,
Ekyune Kim, and Youngjeon Lee, and Hyun-Ju Lee, and Ji Su Kim, and Bong-Seok Song, and Jae-Won Huh, and Sang-Rae Lee, and Sun-Uk Kim, and Sang-Hyun Kim, and Yonggeun Hong, and Insop Shim, and Kyu-Tae Chang
December 2011, Traffic (Copenhagen, Denmark),
Ekyune Kim, and Youngjeon Lee, and Hyun-Ju Lee, and Ji Su Kim, and Bong-Seok Song, and Jae-Won Huh, and Sang-Rae Lee, and Sun-Uk Kim, and Sang-Hyun Kim, and Yonggeun Hong, and Insop Shim, and Kyu-Tae Chang
January 2021, Ibrain,
Copied contents to your clipboard!