Exocytotic fusion is activated by Rab3a peptides

Article Abstract:

Investigation of mammalian and yeast systems have shown that the Rab family of guanosine triphosphate (GTP)-binding proteins are regulators of cell membrane fusion. GTP inhibits GTP-gammaS-induced degranulation which indicates that membrane fusion will result from sustained activation of a GTP-binding protein. Complete exocytotic degranulation similar to that resulting from GTP-gammaS has been found to result from oligopeptides similar to part of the effector domain of Rab3a. Taken with other data this suggests that sustained activation of a Rab3 protein is sufficient for exocytotic fusion.

Cell membranes, Membrane fusion

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GTPase traffic control

Article Abstract:

A new study reveals a new candidate effector for CDc42, one of the Rho-family proteins. A surprise finding is that this subunit may be one of the previously elusive effectors governing Cdc42's impulse to induce cells to grow malignantly and uncontrollably.

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The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation

Article Abstract:

A study reveals a new candidate effector for CDc42, one of the Rho-family proteins. A surprise finding is that this subunit may be one of the previously elusive effectors governing Cdc42's impulse to induce cells to grow malignantly and uncontrollably.

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