The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
TBC1D16 is a Rab4A GTPase activating protein that regulates receptor recycling and EGF receptor signaling
Abstract
Rab4A is a master regulator of receptor recycling from endocytic compartments to the plasma membrane. The protein TBC1D16 is up-regulated in melanoma, and TBC1D16-overexpressing melanoma cells are dependent on TBC1D16. We show here that TBC1D16 enhances the intrinsic rate of GTP hydrolysis by Rab4A. TBC1D16 is both cytosolic and membrane associated; the membrane-associated pool colocalizes with transferrin and EGF receptors (EGFRs) and early endosome antigen 1, but not with LAMP1 protein. Expression of two TBC1D16 isoforms, but not the inactive R494A mutant, reduces transferrin receptor recycling but has no effect on transferrin receptor internalization. Expression of TBC1D16 alters GFP-Rab4A membrane localization. In HeLa cells, overexpression of TBC1D16 enhances EGF-stimulated EGFR degradation, concomitant with decreased EGFR levels and signaling. Thus, TBC1D16 is a GTPase activating protein for Rab4A that regulates transferrin receptor recycling and EGFR trafficking and signaling.
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The accumulation of EGF in a RAB4-positive recycling compartment upon pathogenic LRRK2 expression or RNAi of either RAB8A or RAB10 reflects a crosstalk between recycling and degradative trafficking pathways.
“The accumulation of EGF in a RAB4-positive recycling compartment upon pathogenic LRRK2 expression or RNAi of either RAB8A or RAB10 reflects a crosstalk between recycling and degradative trafficking pathways, which has been described before [64,65,66].”
From Distinct Roles for RAB10 and RAB29 in Pathogenic LRRK2-Mediated Endolysosomal Trafficking Alterations (2020) · cites this paper as [66]
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TBC proteins: GAPs for mammalian small GTPase Rab?
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Rab Proteins and the Compartmentalization of the Endosomal System
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Transcriptomic analyses reveal rhythmic and CLOCK-driven pathways in human skeletal muscle
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Metadata
- Authors
- Goueli, B. S., Powell, M. B., Finger, E. C., & Pfeffer, S. R.
- Affiliations
- Department of Biochemistry, and
- Division of Radiation and Cancer Biology, Department of Radiation Oncology, Stanford University School of Medicine, Stanford, CA 94305
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2012-09-10
- Volume
- 109
- Issue
- 39
- Pages
- 15787-15792
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 41
- References
- 4
- Language
- en
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