Journal article
A phosphatidylinositol 4,5-bisphosphate-sensitive casein kinase I alpha associates with synaptic vesicles and phosphorylates a subset of vesicle proteins
The Journal of cell biology, v 130(3), pp 711-724
01 Aug 1995
PMID: 7622570
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
In interphase cells, alpha-casein kinase I (alpha-CKI) is found associated with cytosolic vesicular structures, the centrosome, and within the nucleus. To identify the specific vesicular structures with which alpha-CKI is associated, established cell lines and primary rat neurons were immunofluorescently labeled with an antibody raised to alpha-CKI. In nonneuronal cells, alpha-CKI colocalizes with vesicular structures which align with microtubules and are partially coincident with both Golgi and endoplasmic reticulum markers. In neurons, alpha-CKI colocalizes with synaptic vesicle markers. When synaptic vesicles were purified from rat brain, they were highly enriched in a CKI, based on activity and immunoreactivity. The synaptic vesicle-associated CKI is an extrinsic kinase and was eluted from synaptic vesicles and purified. This purified CKI has properties most similar to alpha-CKI. When the activities of casein kinase I or II were specifically inhibited on isolated synaptic vesicles, CKI was shown to phosphorylate a specific subset of vesicle proteins, one of which was identified as the synaptic vesicle-specific protein SV2. As with alpha-CKI, the synaptic vesicle CKI is inhibited by phosphatidylinositol 4,5-bisphosphate (PIP2). However, synthesis of PIP2 was detected only in plasma membrane-containing fractions. Therefore, PIP2 may spatially regulate CKI. Since PIP2 synthesis is required for secretion, this inhibition of CKI may be important for the regulation of secretion.
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Details
- Title
- A phosphatidylinositol 4,5-bisphosphate-sensitive casein kinase I alpha associates with synaptic vesicles and phosphorylates a subset of vesicle proteins
- Creators
- S D Gross - Department of Pharmacology, University of Wisconsin Medical School, Madison 53706, USAD P Hoffman - Department of Pharmacology, University of Wisconsin Medical School, Madison 53706, USAP L Fisette - Department of Pharmacology, University of Wisconsin Medical School, Madison 53706, USAP Baas - Department of Pharmacology, University of Wisconsin Medical School, Madison 53706, USAR A Anderson - Department of Pharmacology, University of Wisconsin Medical School, Madison 53706, USA
- Publication Details
- The Journal of cell biology, v 130(3), pp 711-724
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Neurobiology and Anatomy
- Web of Science ID
- WOS:A1995RL49600019
- Scopus ID
- 2-s2.0-0029086047
- Other Identifier
- 991014878066404721
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- Web of Science research areas
- Cell Biology