期刊
JOURNAL OF CELL BIOLOGY
卷 167, 期 1, 页码 43-50出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200406020
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资金
- NCI NIH HHS [P01 CA046128, CA 46128] Funding Source: Medline
- NIMH NIH HHS [F32 MH 067385, F32 MH067385] Funding Source: Medline
- NINDS NIH HHS [R37 NS036251, NS 36251, R01 NS036251, NS 037823] Funding Source: Medline
Talin, an adaptor between integrin and the actin cytoskeleton at sites of cell adhesion, was recently found to be present at neuronal synapses, where its function remains unknown. Talin interacts with pkosphatidylinositol-(4)-phosphate 5-kinase type Igamma, the major phosphatidylinositol-(4,5)-bisphosphate [Pl(4,5)P-2]-synthesizing enzyme in brain. To gain insight into the synaptic role of talin, we microinjected into the large lamprey axons reagents that compete the talin-PIP kinase interaction and then examined their effects on synaptic structure. A dramatic decrease of synaptic actin and an impairment of clathrin-mediated synaptic vesicle endocytosis were observed. The endocytic defect included an accumulation of clathrin-coated pits with wide necks, as previously observed after perturbing actin at these synapses. Thus, the interaction of PIP kinase with talin in presynaptic compartments provides a mechanism to coordinate Pl(4,5)P-2 synthesis, actin dynamics, and endocytosis, and further supports a functional link between actin and clathrin-mediated endocytosis.
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