Mammalian GRIP domain proteins differ in their membrane binding properties and are recruited to distinct domains of the TGN.
about
Retrograde transport pathways utilised by viruses and protein toxinsA functional role for the GCC185 golgin in mannose 6-phosphate receptor recycling.Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185.Differential effects of depletion of ARL1 and ARFRP1 on membrane trafficking between the trans-Golgi network and endosomesTransport Vesicle Tethering at the Trans Golgi Network: Coiled Coil Proteins in ActionDirect imaging of RAB27B-enriched secretory vesicle biogenesis in lacrimal acinar cells reveals origins on a nascent vesicle budding siteGMx33 associates with the trans-Golgi matrix in a dynamic manner and sorts within tubules exiting the Golgi.Tales of tethers and tentacles: golgins in plants.Phosphorylation by casein kinase 2 induces PACS-1 binding of nephrocystin and targeting to cilia.GTP-binding-defective ARL4D alters mitochondrial morphology and membrane potential.Protein flexibility is required for vesicle tethering at the Golgi.Arfaptin-1 negatively regulates Arl1-mediated retrograde transportGCC185 plays independent roles in Golgi structure maintenance and AP-1-mediated vesicle tethering.The small G protein Arl1 directs the trans-Golgi-specific targeting of the Arf1 exchange factors BIG1 and BIG2.The golgin GCC88 is required for efficient retrograde transport of cargo from the early endosomes to the trans-Golgi network.Role of tethering factors in secretory membrane traffic.Multiple Rab GTPase binding sites in GCC185 suggest a model for vesicle tethering at the trans-Golgi.Role of vesicle tethering factors in the ER-Golgi membrane traffic.Entry at the trans-face of the Golgi.The regulation of endosome-to-Golgi retrograde transport by tethers and scaffolds.COPII and COPI traffic at the ER-Golgi interface.Differential sorting and Golgi export requirements for raft-associated and raft-independent apical proteins along the biosynthetic pathway.Dysregulated Arl1, a regulator of post-Golgi vesicle tethering, can inhibit endosomal transport and cell proliferation in yeast.Molecular basis of insulin-responsive GLUT4 trafficking systems revealed by single molecule imaging.Commonly used trafficking blocks disrupt ARF1 activation and the localization and function of specific Golgi proteins.Golgi tethering factor golgin-97 suppresses breast cancer cell invasiveness by modulating NF-κB activity.Activation of ADP-ribosylation factor regulates biogenesis of the ATP7A-containing trans-Golgi network compartment and its Cu-induced traffickingGolgin-97 Targets Ectopically Expressed Inward Rectifying Potassium Channel, Kir2.1, to the -Golgi Network in COS-7 Cells
P2860
Q21245139-F2E9E787-AFE3-416E-9CD8-52CA7CEA2CB4Q24298734-FBC6EA16-DB1A-4D96-A98F-0647E237307BQ24310137-F9C06472-AC83-47BA-ABCD-26731CC5F7F8Q24312046-B7B241EC-88A4-4B14-BCF2-1BA536823631Q26750819-E35E9345-BE74-46DA-A934-2EC4A5EDDF92Q27308870-A70C3F18-13E1-498F-B7B7-56C393CD56ABQ28566265-0BA8CDBF-EFED-44FA-84E0-016F2DC5A700Q34275325-2349AAB5-8B48-481F-B0E9-5B93956F6515Q34324921-48F14FB4-4BDF-4EF0-AB50-CCE34612F388Q34395820-26AF2AA4-13DE-4F07-83F2-B9C5013E307BQ34504670-7209937F-951B-4082-9ACA-6E91FBEC074AQ35196021-039FB529-506C-4117-A58B-1A3D3AC58CBEQ35208471-20BD4BAD-9570-4E8E-BE12-217E02C80ABFQ35744541-2ED92D81-1847-45B0-ABFE-674C5C372ECBQ36173925-F301ED03-5B74-4640-A20E-EF8E2325ED72Q36336697-491F2F64-CD6B-45B1-BFF9-7B6AAF5AE58AQ37035166-3D023AEF-16F3-4C09-9957-FC76361C0A56Q37626903-891E4CF6-DBFD-47F9-8C36-38964FFE1DDAQ37855344-F148516E-CD87-4359-A8D6-2CC23DCEC5D7Q37863216-255E03D5-070F-44B6-BBC9-E129CDABF3B6Q37947559-8E38A58C-2F7B-4764-AEA8-4CC8A3C6B5D5Q39599824-B0D69606-D449-4E0F-BB95-54C40ACE88D0Q42784055-D56F0F0F-3E5B-40C4-B544-55A60A1AD6BBQ42805723-B4176F7D-BE88-457B-B343-1E63DD8C1428Q50422414-9C20CCBE-981B-44BA-8914-E200A930AFA1Q52716161-29B3E092-2F8E-4725-8FFE-EE4708BB11A9Q57405617-88A624F9-8894-4DD8-ACCA-684FAA7676EDQ58801806-3D4EAAFB-DFB2-4C37-BC1F-0556FB6DD501
P2860
Mammalian GRIP domain proteins differ in their membrane binding properties and are recruited to distinct domains of the TGN.
description
2004 nî lūn-bûn
@nan
2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Mammalian GRIP domain proteins ...... o distinct domains of the TGN.
@ast
Mammalian GRIP domain proteins ...... o distinct domains of the TGN.
@en
Mammalian GRIP domain proteins ...... o distinct domains of the TGN.
@nl
type
label
Mammalian GRIP domain proteins ...... o distinct domains of the TGN.
@ast
Mammalian GRIP domain proteins ...... o distinct domains of the TGN.
@en
Mammalian GRIP domain proteins ...... o distinct domains of the TGN.
@nl
prefLabel
Mammalian GRIP domain proteins ...... o distinct domains of the TGN.
@ast
Mammalian GRIP domain proteins ...... o distinct domains of the TGN.
@en
Mammalian GRIP domain proteins ...... o distinct domains of the TGN.
@nl
P2093
P50
P356
P1476
Mammalian GRIP domain proteins ...... o distinct domains of the TGN.
@en
P2093
Catherine van Vliet
Merran C Derby
Michael R Luke
Wanjin Hong
P304
P356
10.1242/JCS.01497
P407
P577
2004-11-02T00:00:00Z