ArticleThe Journal of biological chemistry2012
RUTBC2 protein, a Rab9A effector and GTPase-activating protein for Rab36.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 30 citations in OpenAlex.
- Structural and functional insights into TBC1D17 highlight the importance of the previously uncharacterized Rab-binding domain.Protein science : a publication of the Protein Society · 2026Article
- The Functions of RAB GTPases at the Golgi Complex.Sub-cellular biochemistry · 2026Review
- TBC1D22B Regulates ER-to-Golgi Trafficking via RAB1B Inactivation and Promotes Oncogenic Programs in Breast Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The Role of Rab GTPases in the development of genetic and malignant diseases.Molecular and cellular biochemistry · 2024Review
- Exploring the consequences of redirecting an exocytic Rab onto endocytic vesicles.Molecular biology of the cell · 2023Article
- The PripA-TbcrA complex-centered Rab GAP cascade facilitates macropinosome maturation in Dictyostelium.Nature communications · 2022Article
- Rab GTPases: The principal players in crafting the regulatory landscape of endosomal trafficking.Computational and structural biotechnology journal · 2022Review
- Establishment of an Endocytosis-Related Prognostic Signature for Patients With Low-Grade Glioma.Frontiers in genetics · 2021Article
- High-Throughput Assay for Profiling the Substrate Specificity of Rab GTPase-Activating Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Newer Methods Drive Recent Insights into Rab GTPase Biology: An Overview.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Small G protein signalling modulator 2 (SGSM2) is involved in oestrogen receptor-positive breast cancer metastasis through enhancement of migratory cell adhesion via interaction with E-cadherin.Cell adhesion & migration · 2019Article
- Cytomegaloviruses Exploit Recycling Rab Proteins in the Sequential Establishment of the Assembly Compartment.Frontiers in cell and developmental biology · 2018Review
- Mechanisms and functions of lysosome positioning.Journal of cell science · 2016Review
- Recycling Endosomes and Viral Infection.Viruses · 2016Review
- Identification of a Rab GTPase-activating protein cascade that controls recycling of the Rab5 GTPase Vps21 from the vacuole.Molecular biology of the cell · 2015Article
- Expression and intracellular localization of TBC1D9, a Rab GTPase-accelerating protein, in mouse testes.Experimental animals · 2015Article
- Rab family of GTPases.Methods in molecular biology (Clifton, N.J.) · 2015Review
- Molecular modeling and molecular dynamics simulation study of the human Rab9 and RhoBTB3 C-terminus complex.Bioinformation · 2014Article
- Phosphorylation of the Rab exchange factor Sec2p directs a switch in regulatory binding partners.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Rab GTPase regulation of membrane identity.Current opinion in cell biology · 2013Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Rab GTPases regulate vesicle budding, motility, docking, and fusion. In cells, their cycling between active, GTP-bound states and inactive, GDP-bound states is regulated by the action of opposing enzymes called guanine nucleotide exchange factors and GTPase-activating proteins (GAPs). The substrates for most RabGAPs are unknown, and the potential for cross-talk between different membrane trafficking pathways remains uncharted territory. Rab9A and its effectors regulate recycling of mannose 6-phosphate receptors from late endosomes to the trans Golgi network. We show here that RUTBC2 is a TBC domain-containing protein that binds to Rab9A specifically both in vitro and in cultured cells but is not a GAP for Rab9A. Biochemical screening of Rab protein substrates for RUTBC2 revealed highest GAP activity toward Rab34 and Rab36. In cells, membrane-associated RUTBC2 co-localizes with Rab36, and expression of wild type RUTBC2, but not the catalytically inactive, RUTBC2 R829A mutant, decreases the amount of membrane-associated Rab36 protein. These data show that RUTBC2 can act as a Rab36 GAP in cells and suggest that RUTBC2 links Rab9A function to Rab36 function in the endosomal system.
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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.