FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2262071732> ?p ?o ?g. }

• W2262071732 endingPage "29021" @default.
• W2262071732 startingPage "29010" @default.
• W2262071732 abstract "PI(4,5)P2 localizes to sites of dense core vesicle exocytosis in neuroendocrine cells and is required for Ca2+-triggered vesicle exocytosis, but the impact of local PI(4,5)P2 hydrolysis on exocytosis is poorly understood. Previously, we reported that Ca2+-dependent activation of phospholipase Cη2 (PLCη2) catalyzes PI(4,5)P2 hydrolysis, which affected vesicle exocytosis by regulating the activities of the lipid-dependent priming factors CAPS (also known as CADPS) and ubiquitous Munc13-2 in PC12 cells. Here we describe an additional role for PLCη2 in vesicle exocytosis as a Ca2+-dependent regulator of the actin cytoskeleton. Depolarization of neuroendocrine PC12 cells with 56 or 95 mm KCl buffers increased peak Ca2+ levels to ∼400 or ∼800 nm, respectively, but elicited similar numbers of vesicle exocytic events. However, 56 mm K+ preferentially elicited the exocytosis of plasma membrane-resident vesicles, whereas 95 mm K+ preferentially elicited the exocytosis of cytoplasmic vesicles arriving during stimulation. Depolarization with 95 mm K+ but not with 56 mm K+ activated PLCη2 to catalyze PI(4,5)P2 hydrolysis. The decrease in PI(4,5)P2 promoted F-actin disassembly, which increased exocytosis of newly arriving vesicles. Consistent with its role as a Ca2+-dependent regulator of the cortical actin cytoskeleton, PLCη2 localized with F-actin filaments. The results highlight the importance of PI(4,5)P2 for coordinating cytoskeletal dynamics with vesicle exocytosis and reveal a new role for PLCη2 as a Ca2+-dependent regulator of F-actin dynamics and vesicle trafficking. PI(4,5)P2 localizes to sites of dense core vesicle exocytosis in neuroendocrine cells and is required for Ca2+-triggered vesicle exocytosis, but the impact of local PI(4,5)P2 hydrolysis on exocytosis is poorly understood. Previously, we reported that Ca2+-dependent activation of phospholipase Cη2 (PLCη2) catalyzes PI(4,5)P2 hydrolysis, which affected vesicle exocytosis by regulating the activities of the lipid-dependent priming factors CAPS (also known as CADPS) and ubiquitous Munc13-2 in PC12 cells. Here we describe an additional role for PLCη2 in vesicle exocytosis as a Ca2+-dependent regulator of the actin cytoskeleton. Depolarization of neuroendocrine PC12 cells with 56 or 95 mm KCl buffers increased peak Ca2+ levels to ∼400 or ∼800 nm, respectively, but elicited similar numbers of vesicle exocytic events. However, 56 mm K+ preferentially elicited the exocytosis of plasma membrane-resident vesicles, whereas 95 mm K+ preferentially elicited the exocytosis of cytoplasmic vesicles arriving during stimulation. Depolarization with 95 mm K+ but not with 56 mm K+ activated PLCη2 to catalyze PI(4,5)P2 hydrolysis. The decrease in PI(4,5)P2 promoted F-actin disassembly, which increased exocytosis of newly arriving vesicles. Consistent with its role as a Ca2+-dependent regulator of the cortical actin cytoskeleton, PLCη2 localized with F-actin filaments. The results highlight the importance of PI(4,5)P2 for coordinating cytoskeletal dynamics with vesicle exocytosis and reveal a new role for PLCη2 as a Ca2+-dependent regulator of F-actin dynamics and vesicle trafficking." @default.
• W2262071732 created "2016-06-24" @default.
• W2262071732 creator A5035203566 @default.
• W2262071732 creator A5046406495 @default.
• W2262071732 creator A5049991871 @default.
• W2262071732 date "2015-11-01" @default.
• W2262071732 modified "2023-09-26" @default.
• W2262071732 title "Phospholipase Cη2 Activation Redirects Vesicle Trafficking by Regulating F-actin" @default.
• W2262071732 cites W1568836035 @default.
• W2262071732 cites W1576360313 @default.
• W2262071732 cites W1911645964 @default.
• W2262071732 cites W1956143364 @default.
• W2262071732 cites W1964927812 @default.
• W2262071732 cites W1973220447 @default.
• W2262071732 cites W1973769128 @default.
• W2262071732 cites W1975852922 @default.
• W2262071732 cites W1982448290 @default.
• W2262071732 cites W1982630258 @default.
• W2262071732 cites W1984540625 @default.
• W2262071732 cites W1986861517 @default.
• W2262071732 cites W1992215989 @default.
• W2262071732 cites W2001417653 @default.
• W2262071732 cites W2001780088 @default.
• W2262071732 cites W2007949464 @default.
• W2262071732 cites W2010719811 @default.
• W2262071732 cites W2012683464 @default.
• W2262071732 cites W2017295712 @default.
• W2262071732 cites W2017694247 @default.
• W2262071732 cites W2022099573 @default.
• W2262071732 cites W2023712216 @default.
• W2262071732 cites W2026862088 @default.
• W2262071732 cites W2028553251 @default.
• W2262071732 cites W2031057786 @default.
• W2262071732 cites W2035070093 @default.
• W2262071732 cites W2048465987 @default.
• W2262071732 cites W2056550783 @default.
• W2262071732 cites W2058712930 @default.
• W2262071732 cites W2059637730 @default.
• W2262071732 cites W2060980311 @default.
• W2262071732 cites W2062221283 @default.
• W2262071732 cites W2062516092 @default.
• W2262071732 cites W2064731387 @default.
• W2262071732 cites W2064786640 @default.
• W2262071732 cites W2064968576 @default.
• W2262071732 cites W2072530403 @default.
• W2262071732 cites W2076923427 @default.
• W2262071732 cites W2084310680 @default.
• W2262071732 cites W2091701502 @default.
• W2262071732 cites W2093160716 @default.
• W2262071732 cites W2098143417 @default.
• W2262071732 cites W2098349937 @default.
• W2262071732 cites W2099433102 @default.
• W2262071732 cites W2106723144 @default.
• W2262071732 cites W2107625881 @default.
• W2262071732 cites W2111620983 @default.
• W2262071732 cites W2111904037 @default.
• W2262071732 cites W2113959625 @default.
• W2262071732 cites W2123836140 @default.
• W2262071732 cites W2124440466 @default.
• W2262071732 cites W2133229697 @default.
• W2262071732 cites W2133603739 @default.
• W2262071732 cites W2134782454 @default.
• W2262071732 cites W2138936877 @default.
• W2262071732 cites W2156422809 @default.
• W2262071732 cites W2157465643 @default.
• W2262071732 cites W2165448884 @default.
• W2262071732 cites W2172291224 @default.
• W2262071732 cites W2200436150 @default.
• W2262071732 doi "https://doi.org/10.1074/jbc.m115.658328" @default.
• W2262071732 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4661413" @default.
• W2262071732 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26432644" @default.
• W2262071732 hasPublicationYear "2015" @default.
• W2262071732 type Work @default.
• W2262071732 sameAs 2262071732 @default.
• W2262071732 citedByCount "5" @default.
• W2262071732 countsByYear W22620717322015 @default.
• W2262071732 countsByYear W22620717322016 @default.
• W2262071732 countsByYear W22620717322017 @default.
• W2262071732 countsByYear W22620717322018 @default.
• W2262071732 countsByYear W22620717322020 @default.
• W2262071732 crossrefType "journal-article" @default.
• W2262071732 hasAuthorship W2262071732A5035203566 @default.
• W2262071732 hasAuthorship W2262071732A5046406495 @default.
• W2262071732 hasAuthorship W2262071732A5049991871 @default.
• W2262071732 hasBestOaLocation W22620717321 @default.
• W2262071732 hasConcept C12554922 @default.
• W2262071732 hasConcept C125705527 @default.
• W2262071732 hasConcept C130316041 @default.
• W2262071732 hasConcept C142669718 @default.
• W2262071732 hasConcept C148785051 @default.
• W2262071732 hasConcept C1491633281 @default.
• W2262071732 hasConcept C165254790 @default.
• W2262071732 hasConcept C175969161 @default.
• W2262071732 hasConcept C185592680 @default.
• W2262071732 hasConcept C196330066 @default.
• W2262071732 hasConcept C2909863526 @default.
• W2262071732 hasConcept C2993400109 @default.
• W2262071732 hasConcept C4141045 @default.

• next