期刊
MOLECULAR BIOLOGY OF THE CELL
卷 27, 期 1, 页码 90-107出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E15-06-0329
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资金
- Biotechnology and Biological Sciences Research Council
- Wellcome Trust [086810]
- Medical Research Council Research Grant [MR/K000810/1]
- Lowe Syndrome Trust Grant IC/ICAP
- EPSRC [EP/K039946/1] Funding Source: UKRI
- MRC [MR/K000810/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/K039946/1] Funding Source: researchfish
- Medical Research Council [MR/K000810/1] Funding Source: researchfish
Mutation of the inositol 5-phosphatase OCRL1 causes Lowe syndrome and Dent-2 disease. Loss of OCRL1 function perturbs several cellular processes, including membrane traffic, but the underlying mechanisms remain poorly defined. Here we show that OCRL1 is part of the membrane-trafficking machinery operating at the trans-Golgi network (TGN)/endosome interface. OCRL1 interacts via IPIP27A with the F-BAR protein pacsin 2. OCRL1 and IPIP27A localize to mannose 6-phosphate receptor (MPR)-containing trafficking intermediates, and loss of either protein leads to defective MPR carrier biogenesis at the TGN and endosomes. OCRL1 5-phosphatase activity, which is membrane curvature sensitive, is stimulated by IPIP27A-mediated engagement of OCRL1 with pacsin 2 and promotes scission of MPR-containing carriers. Our data indicate a role for OCRL1, via IPIP27A, in regulating the formation of pacsin 2-dependent trafficking intermediates and reveal a mechanism for coupling PtdIns(4,5)P-2 hydrolysis with carrier biogenesis on endomembranes.
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