Critical to the success of such self-repair paradigms is the effective expansion and recruitment of NPCs to sites of injury or disease. Although SE NPC expansion occurs following injury alone, or in combination with exogenous factors, only a subpopulation of the newly formed NPCs migrate toward lesion sites in response to these stimulants. Augmentation of neurorepair processes may be achieved by enhancing the numbers of SE-derived NPCs that are recruited to lesion sites, and our findings suggest that this may be accomplished with the application of external dcEFs as guidance cues for NPC migration. Our current view of membrane traffic is far from that of a distribution network with machinery that passively responds to the tasks of cargo collection and transport. Elucidation of the molecular mechanisms that regulate the production and consumption of transport carriers is a significant challenge in cell biology, and is central to understanding the underlying contribution of membrane traffic to topics as diverse as apico-basolateral polarity and cell proliferation, how organelles can be manipulated by pathogens to facilitate intracellular entry and residence, and the modulation of cellular morphology during development to generate cell-type specificity. Each stage of transport is expected to be under the control of a variety of different signals requiring regulatory checks and balances and coordination with other cellular events. The Rab family of GTPases are central players in the regulation of membrane traffic. Rab GTPases exert control by harnessing the conformational changes associated with GTP binding and hydrolysis to a cycle of transition between membranes and cytosol. At least one or more Rab family members are a necessary component of all transport steps in the secretory and endocytic systems. Because phosphorylation is a general regulatory modification utilized by diverse signal transduction pathways, its presence on Rab proteins represents a possible intervention point to understand the mechanisms by which membrane traffic is coordinated with other cellular pathways. Several global studies of the yeast phosphoproteome have been performed, identifying sites of phosphorylation on three Rab proteins, Sec4p, Ypt1p and Vps21p. In particular, the Sec4p GTPase has been identified as a multi-site phosphoprotein by two independent studies. Sec4p contains 4�C5 serine phosphorylation sites situated within two stretches close to the NH2 and COOHtermini. In this study we have investigated the consequence of this modification for Sec4p function. Sec4p is encoded by an essential gene and is a critical mediator for the pathway that delivers post-Golgi vesicles to the plasma membrane. This trafficking step is spatially and temporally regulated to the sites of active growth. Reflecting this fact, Sec4p is found at the tip of newly growing cells and at the neck region between dividing cells. The closest mammalian orthologs of Sec4p are Rab8 and Rab13, and these proteins also regulate post-Golgi trafficking pathways. The consequences of Rab GTPase activation are transmitted to downstream effectors, proteins or protein complexes that bind to the nucleotide-activated or GTP-bound conformation of a specific Rab protein. Several effectors have been identified for Sec4p including Sec15p, a member of the octameric exocyst complex. The exocyst complex is also an effector for other Ras-related small GTPases, and is known to be a central player that serves as an intersection point.

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