The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Phosphoinositides in membrane traffic at the synapse
Abstract
Inositol phospholipids represent a minor fraction of membrane phospholipids; yet they play important regulatory functions in signaling pathways and membrane traffic. The phosphorylated inositol ring can act either as a precursor for soluble intracellular messengers or as a binding site for cytosolic or membrane proteins. Hence, phosphorylation-dephosphorylation of phosphoinositides represents a mechanism for regulation of recruitment to the membrane of coat proteins, cytoskeletal scaffolds or signaling complexes and for the regulation of membrane proteins. Recent work suggests that phosphoinositide metabolism has an important role in membrane traffic at the synapse. PtdIns(4,5)P2 generation is implicated in the secretion of at least a subset of neurotransmitters. Furthermore, PtdIns(4,5)P2 plays a role in the nucleation of clathrin coats and of an actin-based cytoskeletal scaffold at endocytic zones of synapses, and PtdIns(4,5)P2 dephosphorylation accompanies the release of newly formed vesicles from these interactions. Thus, the reversible phosphorylation of inositol phospholipids may be one of the mechanisms governing the timing and vectorial progression of synaptic vesicle membranes during their exocytic-endocytic cycle.
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Cites
Fab1p PtdIns(3)P 5-Kinase Function Essential for Protein Sorting in the Multivesicular Body
Odorizzi, G., Babst, M., & Emr, S. D. (1998) · Cell · doi:10.1016/s0092-8674(00)81707-9 · Cited by 656
Butz, S., Okamoto, M., & Südhof, T. C. (1998) · Cell · doi:10.1016/s0092-8674(00)81736-5 · Cited by 548
Martin, T. F. J. (1998) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.14.1.231 · Cited by 522
Role of the ENTH Domain in Phosphatidylinositol-4,5-Bisphosphate Binding and Endocytosis
Itoh, T., Koshiba, S., Kigawa, T., Kikuchi, A., Yokoyama, S., & Takenawa, T. (2001) · Science · doi:10.1126/science.291.5506.1047 · Cited by 469
Piccolo, a presynaptic zinc finger protein structurally related to bassoon
Fenster, S. D., Chung, W. J., Zhai, R., Cases-Langhoff, C., Voss, B., Garner, A. M., Kaempf, U., Kindler, S., Gundelfinger, E. D., & Garner, C. C. (2000) · Neuron · doi:10.1016/s0896-6273(00)80883-1 · Cited by 295
The Caenorhabditis elegans unc-31 gene affects multiple nervous system-controlled functions
Avery, L., Bargmann, C. I., & Horvitz, H. R. (1993) · Genetics · doi:10.1093/genetics/134.2.455 · Cited by 137
Phospholipid-binding protein domains
Bottomley, M. J., Salim, K., & Panayotou, G. (1998) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s0005-2760(98)00141-6 · Cited by 118
Cited by
PIP2and Proteins: Interactions, Organization, and Information Flow
McLaughlin, S., Wang, J., Gambhir, A., & Murray, D. (2002) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.31.082901.134259 · Cited by 837
Fukazawa, Y., Saitoh, Y., Ozawa, F., Ohta, Y., Mizuno, K., & Inokuchi, K. (2003) · Neuron · doi:10.1016/s0896-6273(03)00206-x · Cited by 695
Actin Assembly and Endocytosis: From Yeast to Mammals
Engqvist-Goldstein, Å. E. Y., & Drubin, D. G. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111401.093127 · Cited by 572
Saheki, Y., & De Camilli, P. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005645 · Cited by 457
The dephosphins: dephosphorylation by calcineurin triggers synaptic vesicle endocytosis
Cousin, M. A., & Robinson, P. J. (2001) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01930-5 · Cited by 330
Metadata
- Authors
- Cremona, O., & Camilli, P. D.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2001-03-15
- Volume
- 114
- Issue
- 6
- Pages
- 1041-1052
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W1956143364
- Cited by
- 326
- References
- 7
- FWCI
- 12.92
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
