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NECAP 1 Regulates AP-2 Interactions to Control Vesicle Size,Number,and Cargo During Clathrin-Mediated Endocytosis
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نویسنده
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ritter b. ,murphy s. ,dokainish h. ,girard m. ,gudheti m.v. ,kozlov g. ,halin m. ,philie j. ,jorgensen e.m. ,gehring k. ,mcpherson p.s.
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منبع
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plos biology - 2013 - دوره : 11 - شماره : 10
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چکیده
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Ap-2 is the core-organizing element in clathrin-mediated endocytosis. during the formation of clathrin-coated vesicles,clathrin and endocytic accessory proteins interact with ap-2 in a temporally and spatially controlled manner,yet it remains elusive as to how these interactions are regulated. here,we demonstrate that the endocytic protein necap 1,which binds to the α-ear of ap-2 through a c-terminal wxxf motif,uses an n-terminal ph-like domain to compete with clathrin for access to the ap-2 β2-linker,revealing a means to allow ap-2-mediated coordination of accessory protein recruitment and clathrin polymerization at sites of vesicle formation. knockdown and functional rescue studies demonstrate that through these interactions,necap 1 and ap-2 cooperate to increase the probability of clathrin-coated vesicle formation and to control the number,size,and cargo content of the vesicles. together,our data demonstrate that necap 1 modulates the ap-2 interactome and reveal a new layer of organizational control within the endocytic machinery. © 2013 ritter et al.
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آدرس
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department of neurology and neurosurgery,montreal neurological institute,mcgill university,montreal,qc,canada,department of biochemistry,boston university school of medicine,boston,ma, United States, department of biochemistry,groupe de recherche axé sur la structure des protéines,mcgill university,montreal,qc, Canada, department of neurology and neurosurgery,montreal neurological institute,mcgill university,montreal,qc, Canada, department of neurology and neurosurgery,montreal neurological institute,mcgill university,montreal,qc, Canada, howard hughes medical institute,department of biology,university of utah,salt lake city,ut,united states,vutara,inc.,salt lake city,ut, United States, department of biochemistry,groupe de recherche axé sur la structure des protéines,mcgill university,montreal,qc, Canada, department of neurology and neurosurgery,montreal neurological institute,mcgill university,montreal,qc, Canada, department of neurology and neurosurgery,montreal neurological institute,mcgill university,montreal,qc, Canada, howard hughes medical institute,department of biology,university of utah,salt lake city,ut, United States, department of biochemistry,groupe de recherche axé sur la structure des protéines,mcgill university,montreal,qc, Canada, department of neurology and neurosurgery,montreal neurological institute,mcgill university,montreal,qc, Canada
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Authors
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