Reference - Detail
RRC ID | 49208 |
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Author | Imai A, Nashida T, Shimomura H. |
Title | Roles of Munc18-3 in amylase release from rat parotid acinar cells. |
Journal | Arch Biochem Biophys |
Abstract |
Several "soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor" (SNARE) proteins have been identified in rat parotid acinar cells, including VAMP-2, syntaxin 4, and SNAP-23. Furthermore, an association between Munc18c (Munc18-3) and syntaxin 4 has been reported. However, the role of Munc18-3 in secretory granule exocytosis on parotid acinar cells remains unclear. In the present study, we investigated the role of Munc18-3 in rat parotid acinar cells. Munc18-3 was localized on the apical plasma membrane where exocytosis occurs and interacted with syntaxin 4. Anti-Munc18-3 antibody dose-dependently decreased isoproterenol (IPR)-induced amylase release from SLO-permeabilized parotid acinar cells. Furthermore, stimulation of the acinar cells with IPR induced translocation of Munc18-3 from the plasma membrane to the cytosol. Munc-18-3 was not phosphorylated by a catalytic subunit of protein kinase (PK) A but phosphorylated by PKC. Treatment of the plasma membrane with PKC but not PKA induced displacement of Munc18-3 from the membrane. The results indicate that Munc18-3 regulates exocytosis in the acinar cells for IPR-induced amylase release and that phosphorylation of Munc18-3 by PKA is not involved in the mechanism. |
Volume | 422(2) |
Pages | 175-82 |
Published | 2004-2-15 |
DOI | 10.1016/j.abb.2003.12.021 |
PII | S0003986103006982 |
PMID | 14759605 |
MeSH | Amylases / biosynthesis Amylases / metabolism* Animals Antibodies / pharmacology Bacterial Proteins Base Sequence Cell Membrane / metabolism Cell Membrane Permeability / drug effects Cell Membrane Permeability / physiology Cyclic AMP-Dependent Protein Kinases / metabolism Cytosol / metabolism Isoproterenol / pharmacology Membrane Proteins / metabolism Molecular Sequence Data Munc18 Proteins Nerve Tissue Proteins* Parotid Gland / cytology Parotid Gland / enzymology Parotid Gland / metabolism* Phosphorylation Protein Kinase C / metabolism Proteins / genetics Proteins / immunology Proteins / metabolism* Qa-SNARE Proteins Rats Secretory Vesicles / metabolism Streptolysins / pharmacology Subcellular Fractions / metabolism Vesicular Transport Proteins* |
IF | 3.391 |
Times Cited | 35 |
WOS Category | BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY |
Resource | |
DNA material | pEF-FLAG-rat Munc18-2 (RDB15178) pEF-FLAG-rat Munc18-3 (RDB15179). |