![]() Hydrolysis activity by a family of proteins known as Rab GTPase activating proteins (GAPs) facilitates conversion of Rab-GTP to Rab-GDP, and the Rab is generally released from membranes to the cytoplasm (reviewed in ( 3)). Upon binding to GTP, Rab proteins recruit their molecular effectors, which are proteins that interact specifically with GTP-bound Rabs and carry out select effector functions. The guanine nucleotide exchange factors (GEFs) of Rab proteins catalyze the exchange of GDP with GTP. The Rab-GTP-binding proteins are molecular switches that can either bind GTP when in an activated state and associate with membranes, or they are inactive, GDP-bound, and mostly localized to the cytoplasm (reviewed in ( 3)). Many proteins regulate these trafficking pathways, with the Ras-like small GTP-binding proteins (Rab-GTP-binding proteins) playing a central role. While some receptors are sorted for lysosomal degradation, other receptors are recycled back to the plasma membrane, either in a direct pathway from EE (fast recycling) or indirectly through the endocytic recycling compartment (ERC) (reviewed in ( 1, 2)). Upon endocytosis, newly internalized vesicles are directed to early endosomes (EE). Overall, our data suggest a model in which Rab35 is a critical upstream regulator of MICAL-L1 and Arf6, while both MICAL-L1 and Arf6 regulate Rab8a function.Įndocytosis is a highly conserved process across species in which nutrients, and lipids are internalized into the cells. Moreover, we demonstrate that Arf6 forms a complex with MICAL-L1 and plays a role in its recruitment to tubular endosomes. Over-expression of active Rab35 impairs the recruitment of MICAL-L1 to tubular recycling endosomes, whereas Rab35 depletion promotes enhanced MICAL-L1 localization to these structures. First, we demonstrate that Rab35 is a MICAL-L1 binding partner in vivo. In this study, we identify two GTP-binding proteins as interaction partners of the endocytic regulatory protein MICAL-L1. Despite our familiarity with many of the key regulatory proteins involved in this process, our understanding of the mode by which these proteins cooperate and the sequential manner in which they function remains limited. A variety of small GTP-binding proteins regulate receptor recycling. Once internalized, receptors can either be degraded or recycled back to the plasma membrane. She welcomes hearing from medical students and residents who are interested in health policy and history.Endocytosis is a conserved process across species in which cell surface receptors and lipids are internalized from the plasma membrane. Raz teaches courses related to health policy and politics in the University of Rochester Program for Public -Health Related Majors. Her most recent book, Abusive Policies: How the American Child Welfare System Lost its Way will be out later in 2020. Her second book, What's Wrong with the Poor? Race, Psychiatry and the War on Poverty (UNC 2013), was a 2015 Choice Outstanding Academic Title. She is the author of The Lobotomy Letters: The Making of American Psychosurgery (University of Rochester 2013), which was awarded the Pressman-Burroughs Wellcome Career Development Award. She completed her residency in Internal Medicine at Yale New Haven Hospital in 2015, followed by a Robert Wood Johnson Clinical Scholars Fellowship at the University of Pennsylvania, focusing on health policy research. Before moving to the US for a postdoctoral fellowship at Yale, she worked at the Tel Aviv Medical Center and volunteered with Physicians for Human Rights. She completed her medical training at Tel Aviv University, from where she also received a PhD in history of medicine. Phelps Professorship in Public Policy and Health, and has been a hospitalist with URMC since 2019. Mical Raz, MD, PhD, MSHP holds the Charles E. ![]()
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