Life Cycle of Rab27: A Monomeric GTPase That Regulates Vesicular Trafficking

This template was adapted from the original submission. Edits were made to enhance scientific accuracy, optimal usability and/or to meet industry-leading design standards for science communication. Rab27 is a small monomeric GTPase that acts as a molecular switch, cycling from an inactive state (GDP-bound) to an active state (GTP-bound). Following expression, Rab27 is post-translationally lipidated by Rab GeranylGeranylTransferase. Auxiliary proteins, i.e. a guanine nucleotide exchange factor (GEF) and a GTPase activating protein (GAP), are required to transition between the two states. Only Rab27-GTP can anchor to vesicles and bind to effector proteins thus regulating membrane secretion.

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