A transmembrane segment determines the steady-state localization of an ion-transporting adenosine triphosphatase
about
Multiple regions within the coxsackievirus and adenovirus receptor cytoplasmic domain are required for basolateral sortingTargeting and trafficking of the human thiamine transporter-2 in epithelial cellsLoss of acidification of anterior prostate fluids in Atp12a-null mutant mice indicates that nongastric H-K-ATPase functions as proton pump in vivoMembrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells.Cytosolic COOH terminus of the peptide transporter PEPT2 is involved in apical membrane localization of the protein.Cell adhesion, polarity, and epithelia in the dawn of metazoans.Trafficking to the apical and basolateral membranes in polarized epithelial cellsThe polarized expression of Na+,K+-ATPase in epithelia depends on the association between beta-subunits located in neighboring cells.Protein phosphatase 2A interacts with the Na,K-ATPase and modulates its trafficking by inhibition of its association with arrestin.Mechanisms regulating tissue-specific polarity of monocarboxylate transporters and their chaperone CD147 in kidney and retinal epitheliaCholesterol-induced protein sorting: an analysis of energetic feasibilitySphingolipid trafficking and protein sorting in epithelial cells.MAL decreases the internalization of the aquaporin-2 water channel.Arrestins and spinophilin competitively regulate Na+,K+-ATPase trafficking through association with a large cytoplasmic loop of the Na+,K+-ATPase.Role of N- and O-glycans in polarized biosynthetic sorting.Dual pulse-chase microscopy reveals early divergence in the biosynthetic trafficking of the Na,K-ATPase and E-cadherinSplice-site A choice targets plasma-membrane Ca2+-ATPase isoform 2 to hair bundles.Exon loss accounts for differential sorting of Na-K-Cl cotransporters in polarized epithelial cellsApical sorting of a voltage- and Ca2+-activated K+ channel alpha -subunit in Madin-Darby canine kidney cells is independent of N-glycosylationThe Apical Localization of Na+, K+-ATPase in Cultured Human Retinal Pigment Epithelial Cells Depends on Expression of the β2 Subunit.Polarized traffic towards the cell surface: how to find the route.The Na+-K+-ATPase as self-adhesion molecule and hormone receptor.Regulation of Transporters and Channels by Membrane-Trafficking Complexes in Epithelial Cells.Multiple cytosolic and transmembrane determinants are required for the trafficking of SCAMP1 via an ER-Golgi-TGN-PM pathway.Tyrosine-dependent basolateral targeting of human connexin43-eYFP in Madin-Darby canine kidney cells can be disrupted by the oculodentodigital dysplasia mutation L90VTransmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum.Identification of a novel apical sorting motif and mechanism of targeting of the M2 muscarinic acetylcholine receptor.Angiotensin-converting enzyme 2 (ACE2), but not ACE, is preferentially localized to the apical surface of polarized kidney cells.The apical targeting signal of the P2Y2 receptor is located in its first extracellular loop.Plasma membrane delivery of the gastric H,K-ATPase: the role of beta-subunit glycosylation.Role of the N-terminal transmembrane region of the multidrug resistance protein MRP2 in routing to the apical membrane in MDCKII cells.A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells.Pancreatic bicarbonate secretion involves two proton pumps.Secretion of Antithrombin Is Converted from Nonpolarized to Apical by Exchanging Its Amino Terminus for That of Apically Secreted Family Members
P2860
Q24291163-11FEBEE9-D248-4DC6-A522-DDC8DC4BCAD8Q28288175-8FA5A8D3-C8FF-4F7F-91A7-9A13846ED722Q28513231-EDC16630-BD32-48D1-A129-920C2EBD9AB5Q30437266-CFCFD34A-0CAC-4B4D-877F-F3E779E1F402Q33221888-5101FBF8-8A42-4EC6-8E0A-183920334CFCQ33340425-2952BBFC-29CE-4A20-A4C6-6E1189906F6FQ33814910-49FC319E-6D39-4B74-863D-EB2E5FEF0DF3Q33913636-1DE731EC-9D6F-46D9-9661-08DA81341B60Q34126404-04198ADC-B2B9-4984-A778-E35BC7F9B051Q34132189-B6BB8A1F-2AF8-4084-9070-A140CBE38F94Q34180735-56021899-293D-4509-AE4E-96841F3375C9Q34922136-3C6D5E76-6009-4B97-B20E-5E4E0C687B7BQ36082230-40A8E76B-8A26-4F1D-8CC5-CE36B0BE387EQ36095777-1568E927-FECA-486C-8004-8E165FF8DF32Q36336692-5096AA6C-32CF-4E69-84DF-9CC789669211Q36337026-27A6AB78-9FFD-4175-8D84-4D51CA17B34CQ36389545-BF99A3DF-BCED-4A1B-BDCD-8ADDFEC9AFA3Q36914236-F288E1BE-006D-4190-9B03-659AB824D454Q37283457-6F9D77DE-E037-4BD7-B798-713D2335B30EQ37319896-61D9CA26-C5EE-4816-8C32-24C3CBAAEBF1Q37631623-6DCC14A9-9298-4EFE-9FC6-8D82DE154FF7Q37952164-88AF7F4F-33BA-40AD-8898-7FCFA9D3D9EEQ39155176-7DB7DB8D-6178-4004-99D4-5B0F5DB68345Q39605257-8E94D545-0F46-4416-9E4D-A6198F77B517Q39782970-939E4D25-D452-4B36-85D2-DD481CB1B0D3Q39994820-712EC76E-8FC8-4EC7-AFCE-A9F50CC1C6E9Q40232973-034409AA-2682-4A33-8397-6A9EE40D5CA2Q40373012-DB3F0CC1-189A-4FB7-A1C8-C77CC40B809DQ40418993-84E74765-9004-4C10-B9ED-D5073F998A2DQ40644199-E414E199-8448-4E60-902F-5C1BA3F7A331Q40725892-A2800BBF-A7CA-485D-A590-A49178C5D828Q40811578-9A82C11C-2C74-455A-A48C-78C10DF85523Q41556981-EDFB5A0D-93FE-417D-9107-1E721B8606EAQ56775260-1583F6D5-2F7E-4D95-9344-5AEF14EFAC4F
P2860
A transmembrane segment determines the steady-state localization of an ion-transporting adenosine triphosphatase
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
@zh
2000年學術文章
@zh-hant
name
A transmembrane segment determ ...... rting adenosine triphosphatase
@ast
A transmembrane segment determ ...... rting adenosine triphosphatase
@en
type
label
A transmembrane segment determ ...... rting adenosine triphosphatase
@ast
A transmembrane segment determ ...... rting adenosine triphosphatase
@en
prefLabel
A transmembrane segment determ ...... rting adenosine triphosphatase
@ast
A transmembrane segment determ ...... rting adenosine triphosphatase
@en
P2093
P2860
P356
P1476
A transmembrane segment determ ...... rting adenosine triphosphatase
@en
P2093
P2860
P304
P356
10.1083/JCB.148.4.769
P407
P577
2000-02-01T00:00:00Z