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Illuminating the functional and structural repertoire of human TBC/RABGAPs

by Frasa, Marieke A. M. , Koessmeier, Katja T. , Braga, Vania M. M. , Ahmadian, M. Reza

in 631/80/313 / 86 / Biochemistry / Biological Transport - genetics / Biological Transport - physiology / Biomedical and Life Sciences / Cancer Research / Cell Biology / Cell Membrane - metabolism / Cells / Cellular proteins / Developmental Biology / GTPase-Activating Proteins - chemistry / GTPase-Activating Proteins - genetics / GTPase-Activating Proteins - metabolism / GTPase-Activating Proteins - physiology / Guanosine triphosphatase / Humans / Life Sciences / Localization / Membranes / Microtubule-Associated Proteins - chemistry / Microtubule-Associated Proteins - genetics / Microtubule-Associated Proteins - metabolism / Microtubule-Associated Proteins - physiology / Models, Biological / Physiological aspects / progress / Protein Interaction Domains and Motifs - genetics / Protein Interaction Domains and Motifs - physiology / Proteins / Research - trends / rho GTP-Binding Proteins - chemistry / rho GTP-Binding Proteins - genetics / rho GTP-Binding Proteins - metabolism / rho GTP-Binding Proteins - physiology / Stem Cells / Structure-Activity Relationship / Teaching

2012

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Illuminating the functional and structural repertoire of human TBC/RABGAPs

by Frasa, Marieke A. M. , Koessmeier, Katja T. , Braga, Vania M. M. , Ahmadian, M. Reza

2012

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Illuminating the functional and structural repertoire of human TBC/RABGAPs

by Frasa, Marieke A. M. , Koessmeier, Katja T. , Braga, Vania M. M. , Ahmadian, M. Reza

2012

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Journal Article

Illuminating the functional and structural repertoire of human TBC/RABGAPs

Frasa, Marieke A. M.,

Koessmeier, Katja T.,

Braga, Vania M. M.,

Ahmadian, M. Reza

2012

Overview

TBC/RABGAPs are negative regulators of RABs that carry a conserved TBC domain. In addition to their roles in intracellular trafficking, they have recently emerged as integrators of signalling between RABs and other small GTPases, and they are frequently dysregulated in disease. The Tre2–Bub2–Cdc16 (TBC) domain-containing RAB-specific GTPase-activating proteins (TBC/RABGAPs) are characterized by the presence of highly conserved TBC domains and act as negative regulators of RABs. The importance of TBC/RABGAPs in the regulation of specific intracellular trafficking routes is now emerging, as is their role in different diseases. Importantly, TBC/RABGAPs act as key regulatory nodes, integrating signalling between RABs and other small GTPases and ensuring the appropriate retrieval, transport and delivery of different intracellular vesicles.

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Publisher

Nature Publishing Group UK,Nature Publishing Group

Subject

631/80/313

/ 86

/ Biochemistry

/ Biological Transport - genetics

/ Biological Transport - physiology

/ Biomedical and Life Sciences

/ Cancer Research