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Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca2+-activated secretion

Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca2+-activated secretion ELUCIDATION of the reactions responsible for the calcium-regulated fusion of secretory granules with the plasma membrane in secretory cells would be facilitated by the identification of participant proteins having known biochemical activities. The successful characterization of cytosolic1–3 and vesicle4,5 proteins that may function in calcium-regulated secretion has not yet revealed the molecular events underlying this process. Regulated secretion consists of sequential priming and triggering steps which depend on ATP and Ca2+, respectively, and require distinct cytosolic proteins6. Characterization of priming-specific factors (PEP proteins) should enable the ATP-requiring reactions to be identified. Here we show that one of the mammalian priming factors (PEP3) is identical to phosphatidylinositol transfer protein (PITP)7. The physiological role of PITP was previously unknown. We also find that SEC14p, the yeast phosphatidylinositol transfer protein which is essential for constitutive secretion8–10, can substitute for PEP3/PITP in priming. Our results indicate that a role for phospholipid transfer proteins is conserved in the constitutive and regulated secretory pathways. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca2+-activated secretion

Hay, Jesse C.; Martin, Thomas F. J.
Nature , Volume 366 (6455) – Dec 9, 1993
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References (30)

Publisher
Springer Journals
Copyright
Copyright © 1993 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/366572a0
Publisher site
See Article on Publisher Site

Abstract

ELUCIDATION of the reactions responsible for the calcium-regulated fusion of secretory granules with the plasma membrane in secretory cells would be facilitated by the identification of participant proteins having known biochemical activities. The successful characterization of cytosolic1–3 and vesicle4,5 proteins that may function in calcium-regulated secretion has not yet revealed the molecular events underlying this process. Regulated secretion consists of sequential priming and triggering steps which depend on ATP and Ca2+, respectively, and require distinct cytosolic proteins6. Characterization of priming-specific factors (PEP proteins) should enable the ATP-requiring reactions to be identified. Here we show that one of the mammalian priming factors (PEP3) is identical to phosphatidylinositol transfer protein (PITP)7. The physiological role of PITP was previously unknown. We also find that SEC14p, the yeast phosphatidylinositol transfer protein which is essential for constitutive secretion8–10, can substitute for PEP3/PITP in priming. Our results indicate that a role for phospholipid transfer proteins is conserved in the constitutive and regulated secretory pathways.

Journal

Nature – Springer Journals

Published: Dec 9, 1993

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