Parotid Secretory Protein Binds Phosphatidylinositol (3,4) Bisphosphate

Venkatesh, S. G.; Goyal, Dipti; Carenbauer, Anne L.; Darling, Douglas S.

doi:10.1177/0022034511410699

Cited by 11 publications

(27 citation statements)

References 31 publications

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“…However, previous results show both bacterially expressed rat PSP and human PSP synthesized in vitro bind specifically to Phosphatidylinositol (3,4)Bisphosphate [36]. PSP bound to PI(3,4)P2 10-fold stronger than to PtdIns(3,5)P 2 or PtdIns(4)P. The ability of PSP to decorate membranes suggests additional functions and may give us more insight as to how PSP is sorted and secreted.…”

Section: Mechanism Of Parotid Gland Secretionmentioning

confidence: 90%

“…Western blot analysis was done with independent purified samples and confirmed that PSP selectively bound to granule membranes, unlike amylase and ProlineRich Protein (PRP) [36]. When exogenous PSP was tested with digested granule membranes it still bound effectively, indicating that PSP does not require a protein receptor for binding to the membrane.…”

Section: Mechanism Of Parotid Gland Secretionmentioning

confidence: 92%

“…The phosphorylated forms of phosphatidylinositol lipids typically function to anchor proteins to specific membranes. It has been found that both human and rat PSP bind specifically to PI(3,4)P 2 , either in liposome membranes or on lipid-overlay assays [37]. Other experiments suggest that this binding is important for interaction of PSP with secretory granule membranes.…”

Section: Mechanism Of Parotid Gland Secretionmentioning

confidence: 99%

“…There is not a lot of research on the function of PSP, however, we do know that PSP binds to Phosphatidylinositol (3,4)Bisphosphate [37]. Recent research also shows that PSP binds to the sugars of lipopolysaccarides (LPS) [48] and can reduce biofilms confirming antimicrobial activity.…”

Section: Structure Of Pspmentioning

confidence: 99%

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The dimerization of parotid secretory protein.

Blau¹

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Section: Mechanism Of Parotid Gland Secretionmentioning

confidence: 90%

Section: Mechanism Of Parotid Gland Secretionmentioning

confidence: 92%

Section: Mechanism Of Parotid Gland Secretionmentioning

confidence: 99%

Section: Structure Of Pspmentioning

confidence: 99%

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The dimerization of parotid secretory protein.

Blau¹

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“…Cargo proteins secreted into the parotid saliva are transcribed, translated, sorted, stored, and secreted by the parotid acinar cells (Venkatesh, Goyal, Carenbauer, & Darling, 2011). These polarized cells are cone shaped and are found in clusters called acini (Baker, 2010) Figures 1A, 1B.…”

Section: Parotid Gland Acinar Cellsmentioning

confidence: 99%

XBP1 and MIST1 are not sufficient to induce the regulated secretory pathway in parotid cell lines.

Pyle¹,

Ian²

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Multiple roles for the actin cytoskeleton during regulated exocytosis

Porat-Shliom

Milberg

Masedunskas

et al. 2012

Cell. Mol. Life Sci.

167

162

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Regulated exocytosis is the main mechanism utilized by specialized secretory cells to deliver molecules to the cell surface by virtue of membranous containers (i.e. secretory vesicles). The process involves a series of highly coordinated and sequential steps, which include the biogenesis of the vesicles, their delivery to the cell periphery, their fusion with the plasma membrane and the release of their content into the extracellular space. Each of these steps is regulated by the actin cytoskeleton. In this review, we summarize the current knowledge regarding the involvement of actin and its associated molecules during each of the exocytic steps in vertebrates, and suggest that the overall role of the actin cytoskeleton during regulated exocytosis is linked to the architecture and the physiology of the secretory cells under examination. Specifically, in neurons, neuroendocrine, endocrine, and hematopoietic cells, which contain small secretory vesicles that undergo rapid exocytosis (on the order of milliseconds), the actin cytoskeleton plays a role in pre-fusion events, where it acts primarily as a functional barrier and facilitates docking. In exocrine and other secretory cells, which contain large secretory vesicles that undergo slow exocytosis (seconds to minutes), the actin cytoskeleton plays a role in post-fusion events, where it regulates the dynamics of the fusion pore, facilitates the integration of the vesicles into the plasma membrane, provides structural support, and promotes the expulsion of large cargo molecules.

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Parotid Secretory Protein Binds Phosphatidylinositol (3,4) Bisphosphate

Abstract: A supplemental appendix to this article is published electronically only at http://jdr.sagepub.com/supplemental.

Cited by 11 publications

References 31 publications

The dimerization of parotid secretory protein.

The dimerization of parotid secretory protein.

XBP1 and MIST1 are not sufficient to induce the regulated secretory pathway in parotid cell lines.

Multiple roles for the actin cytoskeleton during regulated exocytosis

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