Apical targeting and Golgi retention signals reside within a 9-amino acid sequence in the copper-ATPase, ATP7B.
about
Mutations in VIPAR cause an arthrogryposis, renal dysfunction and cholestasis syndrome phenotype with defects in epithelial polarizationCopper directs ATP7B to the apical domain of hepatic cells via basolateral endosomesIntracellular α(2C)-adrenoceptors: storage depot, stunted development or signaling domain?The role of metal binding and phosphorylation domains in the regulation of cisplatin-induced trafficking of ATP7B.Polarized sorting and trafficking in epithelial cellsInvolvement of protein kinase D in expression and trafficking of ATP7B (copper ATPase)ZP2 and ZP3 cytoplasmic tails prevent premature interactions and ensure incorporation into the zona pellucida.Cellular copper levels determine the phenotype of the Arg875 variant of ATP7B/Wilson disease protein.Critical roles for the COOH terminus of the Cu-ATPase ATP7B in protein stability, trans-Golgi network retention, copper sensing, and retrograde trafficking.Communication between the N and C termini is required for copper-stimulated Ser/Thr phosphorylation of Cu(I)-ATPase (ATP7B).Evolution of copper transporting ATPases in eukaryotic organisms.Molecular events initiating exit of a copper-transporting ATPase ATP7B from the trans-Golgi networkThe CXXC motifs in the metal binding domains are required for ATP7B to mediate resistance to cisplatin.Myosin Vb mediates Cu+ export in polarized hepatocytes.Hepatocyte polarityRole of the P-Type ATPases, ATP7A and ATP7B in brain copper homeostasis.Expression profile and overexpression outcome indicate a role for βKlotho in skeletal muscle fibro/adipogenesis.High yield heterologous expression of wild-type and mutant Cu+-ATPase (ATP7B, Wilson disease protein) for functional characterization of catalytic activity and serine residues undergoing copper-dependent phosphorylation.A stimulus needed for the study of membrane traffic in hepatocytes.Polarized traffic towards the cell surface: how to find the route.Distinct phenotype of a Wilson disease mutation reveals a novel trafficking determinant in the copper transporter ATP7B.Advances in the understanding of mammalian copper transporters.Golgi in copper homeostasis: a view from the membrane trafficking field.Dynamics of the metal binding domains and regulation of the human copper transporters ATP7B and ATP7A.Build them up and break them down: Tight junctions of cell lines expressing typical hepatocyte polarity with a varied repertoire of claudins.In silico modeling of the Menkes copper-translocating P-type ATPase 3rd metal binding domain predicts that phosphorylation regulates copper-binding.The six metal binding domains in human copper transporter, ATP7B: molecular biophysics and disease-causing mutations.The metal chaperone Atox1 regulates the activity of the human copper transporter ATP7B by modulating domain dynamics.
P2860
Q24301355-401D92BD-C990-4AD1-82D9-C8889DDF9860Q27346776-F38F78D3-63E9-406E-8065-5EC88241D81EQ28389791-737ABAE8-1D4B-439B-95A4-9AC93CCB70A6Q33649147-7D75580F-C857-4D05-B7CE-9F062060A141Q34270230-2EEF0180-7F6C-40CA-BCB7-F7C6BAC5B59AQ34606325-62BBE828-0F5D-4B2B-BFC0-E2635D256D99Q34625130-D4448DC2-8C94-4FA3-BF6C-A37B91CB73CFQ34750429-E126444F-EDAE-41E9-9C4A-5D444335467CQ35087086-DA997B6C-BA6E-4BBD-808F-BB37C47AA5B5Q35580770-5C056B6F-4D54-4863-B8FF-1B59E15E33D9Q35841316-648E2CE0-6231-402A-BE67-467D9BA18E64Q36332811-7BAE3C12-8A61-45C2-9F21-95C6260BD429Q36650582-A6CC319E-5CAB-43F3-9C5F-31465CE8D53DQ36743873-897DEB7D-9DC1-4B18-AB55-0D7D1C50E6BBQ36972087-221769F2-B120-4D4C-B6E5-5E3676D1C1ECQ37112824-93F64662-C56A-4039-BD7E-620FC498F0ABQ37351645-F167F193-A4B6-4CC0-8530-BFA65584B040Q37372028-D950B176-01A5-476D-A461-A93532AEC8D9Q37539833-69004A17-9085-453D-BE39-6DC281F24EE3Q37631623-36540DFA-04C1-4C0E-9CB5-D411F7317FCAQ37702034-577B1216-0B73-43EB-A508-302055E92A1CQ37983830-994E5DB5-D987-4AF2-80F4-4730C2D2E5D2Q38121020-A4212240-829B-4C87-8E02-FFDD60C147AAQ39167691-53C9829B-5360-4219-A0D6-3F833795C621Q42131137-1B2B6614-CFC8-4DB5-A886-3D65AB641790Q42755592-B33EE6F8-42F5-4068-BAEC-9D4F65219FC9Q46108156-959703AD-B97A-4089-9D91-A1FDB082FB94Q47814434-737F3EF2-1E68-4A57-8AE5-5428190CB06E
P2860
Apical targeting and Golgi retention signals reside within a 9-amino acid sequence in the copper-ATPase, ATP7B.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Apical targeting and Golgi ret ...... e in the copper-ATPase, ATP7B.
@en
Apical targeting and Golgi ret ...... e in the copper-ATPase, ATP7B.
@nl
type
label
Apical targeting and Golgi ret ...... e in the copper-ATPase, ATP7B.
@en
Apical targeting and Golgi ret ...... e in the copper-ATPase, ATP7B.
@nl
prefLabel
Apical targeting and Golgi ret ...... e in the copper-ATPase, ATP7B.
@en
Apical targeting and Golgi ret ...... e in the copper-ATPase, ATP7B.
@nl
P2093
P2860
P356
P1476
Apical targeting and Golgi ret ...... e in the copper-ATPase, ATP7B.
@en
P2093
Ann Hubbard
Lelita Braiterman
Lydia Nyasae
Rodrigo Bustos
Svetlana Lutsenko
P2860
P304
P356
10.1152/AJPGI.90489.2008
P577
2008-11-25T00:00:00Z