Regular ArticleInvolvement of Rho GTPases and Their Effectors in the Secretory Process of PC12 Cells
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Cited by (35)
New Insights into the Role of the Cortical Cytoskeleton in Exocytosis from Neuroendocrine Cells
2012, International Review of Cell and Molecular BiologyCitation Excerpt :Specifically, RhoA is associated with secretory granules and it is a downstream partner of vesicular-associated Go, a trimeric GTPase that regulates the priming steps of exocytosis (Gasman et al., 1997; Vitale et al., 1996). Activation of RhoA via the Go pathway (Gasman et al., 1997), or expression of a constitutively activated GTP-RhoA mutant, impairs secretion and stabilizes the F-actin cortical barrier in PC12 (Frantz et al., 2002) and chromaffin cells (Bader et al., 2004). The phosphatidylinositol 4-kinase enzyme that associates with chromaffin granules is thought to be the effector mediating RhoA inhibition of secretion (Gasman et al., 1998).
Rho GTPases and exocytosis: What are the molecular links?
2011, Seminars in Cell and Developmental BiologyCitation Excerpt :N-WASP and Arp2/3 initiate actin polymerization once N-WASP is activated upon binding to active Cdc42 and phosphatidyl PIP2 [85]. Overexpression of N-WASP in PC12 cells enhanced secretion [83,86], and the N-WASP mutant unable to stimulate actin polymerization abolished Cdc42-dependent secretion [83]. In addition, since part of the Arp2/3 complex was detected on secretory granules membranes and translocated to the plasma membrane upon stimulation [83], secretagogue-evoked activation of Cdc42/N-WASP complex was proposed to trigger local Ap2/3-dependent actin polymerization at the exocytic sites.
Exocytosis in neuroendocrine cells: New tasks for actin
2006, Biochimica et Biophysica Acta - Molecular Cell ResearchInhibition of the RhoA/Rho kinase system attenuates catecholamine biosynthesis in PC 12 rat pheochromocytoma cells
2005, Biochimica et Biophysica Acta - General SubjectsMyristoylated alanine-rich C kinase substrate-mediated neurotensin release via protein kinase C-δ downstream of the Rho/ROK pathway
2005, Journal of Biological ChemistryCitation Excerpt :Our findings provide direct evidence to suggest the regulation of MARCKS activity by the interaction of PKC and Rho/ROK pathways, culminating in stimulated NT secretion. Both PKC (48-53) and Rho family (54-60) pathways have been separately implicated in the regulation of secretion from neuroendocrine cells; however, the interaction between the two molecules has not been previously reported in neuroendocrine cells. In human neuronal cells, MARCKS phosphorylation at Ser-159 (a site recognized by PKC) is induced by lysophosphatidic acid, interleukin-1β, bradykinin, or GTPγS, which activates Rho protein with the resultant activation of ROK (37, 61, 62).
The role of protein kinase D in neurotensin secretion mediated by protein kinase C-α/-δ and Rho/Rho kinase
2004, Journal of Biological ChemistryCitation Excerpt :In addition, Cdc42 and Rac control regulated secretion in pancreatic β-cells (61). ROK, an effector of Rho proteins but not Rac or Cdc42, is also involved in exocytosis (35, 62). But the mechanisms how Rho family regulates the exocytotic process remains unknown.
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