In vivo phosphorylation of adaptors regulates their interaction with clathrin.
about
A novel AAK1 splice variant functions at multiple steps of the endocytic pathwaySubunit H of the V-ATPase involved in endocytosis shows homology to beta-adaptinsA di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3.The AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with a casein kinase Ialpha-like isoformAdaptins: the final recountThe structure and function of the beta 2-adaptin appendage domainMutations in the gene encoding the Sigma 2 subunit of the adaptor protein 1 complex, AP1S2, cause X-linked mental retardationIdentification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosisPhosphorylation of the AP2 mu subunit by AAK1 mediates high affinity binding to membrane protein sorting signalsDifferential requirements for AP-2 in clathrin-mediated endocytosisMembrane-associated GAIP is a phosphoprotein and can be phosphorylated by clathrin-coated vesiclesAtomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linkerActivation of the MAPK signal cascade by the neural cell adhesion molecule L1 requires L1 internalization.Suppressors of YCK-encoded yeast casein kinase 1 deficiency define the four subunits of a novel clathrin AP-like complex.AAK1-mediated micro2 phosphorylation is stimulated by assembled clathrinInteractions between adaptor protein-1 of the clathrin coat and microtubules via type 1a microtubule-associated proteinsCK2 and GAK/auxilin2 are major protein kinases in clathrin-coated vesiclesBeta3A-adaptin, a subunit of the adaptor-like complex AP-3Clathrin-mediated endocytosis of the beta-adrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1The vesicular acetylcholine transporter interacts with clathrin-associated adaptor complexes AP-1 and AP-2AP180 and AP-2 interact directly in a complex that cooperatively assembles clathrinClathrin promotes centrosome integrity in early mitosis through stabilization of centrosomal ch-TOGBinding of AP2 to sorting signals is modulated by AP2 phosphorylation.The clathrin-binding motif and the J-domain of Drosophila Auxilin are essential for facilitating Notch ligand endocytosis.Chemokine receptor trafficking and viral replication.Plasticity of B cell receptor internalization upon conditional depletion of clathrinA phosphotyrosine switch for cargo sequestration at clathrin-coated buds.Temporal and spatial coordination of exocytosis and endocytosis.Vesicular trafficking machinery, the actin cytoskeleton, and H+-K+-ATPase recycling in the gastric parietal cell.CVAK104 is a novel poly-L-lysine-stimulated kinase that targets the beta2-subunit of AP2.Regulation of endosome sorting by a specific PP2A isoform.Adaptor and clathrin exchange at the plasma membrane and trans-Golgi network.The Ark1/Prk1 family of protein kinases. Regulators of endocytosis and the actin skeleton.ADP-Ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes.Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits.AP-1 binding to sorting signals and release from clathrin-coated vesicles is regulated by phosphorylationG protein-coupled receptor/arrestin3 modulation of the endocytic machineryConformational changes of coat proteins during vesicle formation.Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network.Cluster of differentiation antigen 4 (CD4) endocytosis and adaptor complex binding require activation of the CD4 endocytosis signal by serine phosphorylation
P2860
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P2860
In vivo phosphorylation of adaptors regulates their interaction with clathrin.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
In vivo phosphorylation of adaptors regulates their interaction with clathrin.
@ast
In vivo phosphorylation of adaptors regulates their interaction with clathrin.
@en
type
label
In vivo phosphorylation of adaptors regulates their interaction with clathrin.
@ast
In vivo phosphorylation of adaptors regulates their interaction with clathrin.
@en
prefLabel
In vivo phosphorylation of adaptors regulates their interaction with clathrin.
@ast
In vivo phosphorylation of adaptors regulates their interaction with clathrin.
@en
P2860
P356
P1476
In vivo phosphorylation of adaptors regulates their interaction with clathrin.
@en
P2093
P2860
P304
P356
10.1083/JCB.135.3.635
P407
P577
1996-11-01T00:00:00Z