ArticleThe Journal of biological chemistry2009
Rab2 utilizes glyceraldehyde-3-phosphate dehydrogenase and protein kinase C{iota} to associate with microtubules and to recruit dynein.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 70 citations in OpenAlex.
- Insights in tubulin-like structures of the poultry pathogen Mycoplasmoides gallisepticum.Archives of microbiology · 2026Article
- A Syd and RUFY dynein adaptor complex mediates axonal circulation of dense core vesicles.The Journal of cell biology · 2026Article
- Glycolysis and glycolytic enzymes in acute myeloid leukemia: Warburg and beyond.Frontiers in pharmacology · 2026Review
- Glyceraldehyde-3-phosphate dehydrogenase 7 (FtGAPDH7) confers heat stress tolerance in buckwheat [Fagopyrum tataricum (L.) Gaertn].Plant cell reports · 2025Article
- A dual role of ERGIC-localized Rabs in TMED10-mediated unconventional protein secretion.Nature cell biology · 2024Article
- The uncommon function and mechanism of the common enzyme glyceraldehyde-3-phosphate dehydrogenase in the metamorphosis ofFrontiers in bioengineering and biotechnology · 2022Article
- Susceptibility of cytoskeletal-associated proteins for tumor progression.Cellular and molecular life sciences : CMLS · 2021Review
- Proteomic Analysis ofMolecular & cellular proteomics : MCP · 2020Article
- Moonlighting Proteins Are Important Players in Cancer Immunology.Frontiers in immunology · 2020Review
- Relative quantification of BCL2 mRNA for diagnostic usage needs stable uncontrolled genes as reference.PloS one · 2020Observational
- Regulation of Autophagy by Nuclear GAPDH and Its Aggregates in Cancer and Neurodegenerative Disorders.International journal of molecular sciences · 2019Review
- An Emerging Role for Tubulin Isotypes in Modulating Cancer Biology and Chemotherapy Resistance.International journal of molecular sciences · 2017Review
- Membrane skeletal association and post-translational allosteric regulation of Toxoplasma gondii GAPDH1.Molecular microbiology · 2017Article
- GAPDH binds Akt to facilitate cargo transport in the early secretory pathway.Experimental cell research · 2016Article
- Multifunctional Microtubule-Associated Proteins in Plants.Frontiers in plant science · 2016Review
- Protein Recognition in Drug-Induced DNA Alkylation: When the Moonlight Protein GAPDH Meets S23906-1/DNA Minor Groove Adducts.International journal of molecular sciences · 2015Review
- Critical protein GAPDH and its regulatory mechanisms in cancer cells.Cancer biology & medicine · 2015Review
- Proteomes of host cell membranes modified by intracellular activities of Salmonella enterica.Molecular & cellular proteomics : MCP · 2015Article
- Proteomic study of the brackish water musselZoological studies · 2015Article
- Overexpression of atypical protein kinase C in HeLa cells facilitates macropinocytosis via Src activation.Cellular signalling · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Rab2 requires glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and atypical protein kinase Ciota (aPKCiota) for retrograde vesicle formation from vesicular tubular clusters that sort secretory cargo from recycling proteins returned to the endoplasmic reticulum. However, the precise role of GAPDH and aPKCiota in the early secretory pathway is unclear. GAPDH was the first glycolytic enzyme reported to co-purify with microtubules (MTs). Similarly, aPKC associates directly with MTs. To learn whether Rab2 also binds directly to MTs, a MT binding assay was performed. Purified Rab2 was found in a MT-enriched pellet only when both GAPDH and aPKCiota were present, and Rab2-MT binding could be prevented by a recombinant fragment made to the Rab2 amino terminus (residues 2-70), which directly interacts with GAPDH and aPKCiota. Because GAPDH binds to the carboxyl terminus of alpha-tubulin, we characterized the distribution of tyrosinated/detyrosinated alpha-tubulin that is recruited by Rab2 in a quantitative membrane binding assay. Rab2-treated membranes contained predominantly tyrosinated alpha-tubulin; however, aPKCiota was the limiting and essential factor. Tyrosination/detyrosination influences MT motor protein binding; therefore, we determined whether Rab2 stimulated kinesin or dynein membrane binding. Although kinesin was not detected on membranes incubated with Rab2, dynein was recruited in a dose-dependent manner, and binding was aPKCiota-dependent. These combined results suggest a mechanism by which Rab2 controls MT and motor recruitment to vesicular tubular clusters.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.