Multiple regions contribute to membrane targeting of Rab GTPases.
about
Rab1a and Rab5a preferentially bind to binary lipid compositions with higher stored curvature elastic energyRabGEFs are a major determinant for specific Rab membrane targetingStructural basis for recruitment of RILP by small GTPase Rab7TIP47 is a key effector for Rab9 localizationMolecular Analysis and Localization of CaARA7 a Conventional RAB5 GTPase from Characean Algae.Guanine nucleotide exchange factors (GEFs) have a critical but not exclusive role in organelle localization of Rab GTPases.Bioinformatic and comparative localization of Rab proteins reveals functional insights into the uncharacterized GTPases Ypt10p and Ypt11pA novel statin-mediated "prenylation block-and-release" assay provides insight into the membrane targeting mechanisms of small GTPases.Rab13 Traffics on Vesicles Independent of Prenylation.Phylogeny and evolution of Rab7 and Rab9 proteinsAdaptor protein Ruk/CIN85 is associated with a subset of COPI-coated membranes of the Golgi complex.RAB2A: a major subacrosomal protein of bovine spermatozoa implicated in acrosomal biogenesis.A role for Na+,K+-ATPase α1 in regulating Rab27a localisation on melanosomes.The interaction properties of the human Rab GTPase family--comparative analysis reveals determinants of molecular binding selectivitySemi-automated analysis of organelle movement and membrane content: understanding rab-motor complex transport functionPosttranslational modifications of Rab GTPases help their insertion into membranes.Identification of a Rab GTPase-activating protein cascade that controls recycling of the Rab5 GTPase Vps21 from the vacuole.Rab27a targeting to melanosomes requires nucleotide exchange but not effector bindingMolecular insights into vesicle tethering at the Golgi by the conserved oligomeric Golgi (COG) complex and the golgin TATA element modulatory factor (TMF)Rab3GEP is the non-redundant guanine nucleotide exchange factor for Rab27a in melanocytes.Review series: Rab GTPases and membrane identity: causal or inconsequential?The role of the hypervariable C-terminal domain in Rab GTPases membrane targeting.Rab protein evolution and the history of the eukaryotic endomembrane system.Retrograde vesicle transport in the Golgi.Rab proteins and the secretory pathway: the case of rab18 in neuroendocrine cells.Rab27a and melanosomes: a model to investigate the membrane targeting of Rabs.Rab proteins of the endoplasmic reticulum: functions and interactors.Molecular control of Rab activity by GEFs, GAPs and GDI.A coiled-coil domain of melanophilin is essential for Myosin Va recruitment and melanosome transport in melanocytes.Rab GTPases and their interacting protein partners: Structural insights into Rab functional diversity.Targeting of the Sendai virus C protein to the plasma membrane via a peptide-only membrane anchor.Regulation of human melanocortin 1 receptor signaling and trafficking by Thr-308 and Ser-316 and its alteration in variant alleles associated with red hair and skin cancer.Locking GTPases covalently in their functional states.The Rab interacting lysosomal protein (RILP) homology domain functions as a novel effector domain for small GTPase Rab36: Rab36 regulates retrograde melanosome transport in melanocytes.Consequences of Rab GTPase dysfunction in genetic or acquired human diseases.Recognition and stabilization of geranylgeranylated human Rab5 by the GDP Dissociation Inhibitor (GDI).Dictyostelium RacH regulates endocytic vesicular trafficking and is required for localization of vacuolin.Lrrk2 R1441 substitution and progressive supranuclear palsy
P2860
Q24297143-29AD6378-B2B3-4828-853E-F4FBCDBC15E2Q24314408-33FFC2EE-15F5-4101-B61B-1B8824B7089AQ24529126-CA645E31-362C-4031-BE40-FF59C84C80CDQ24683616-DB4DE9DC-103E-4423-BC61-A3D6195D8CBBQ27346689-16299EFB-65AE-4450-A708-01B2645A33F8Q27934171-A0FAC9CF-A50C-409F-97AC-84DD445D5E8FQ27936497-3B192D93-5E00-4999-A9EA-EE44120B3352Q30495640-02D71E88-3C41-42B0-8A52-5ABED3EFC6F8Q30756731-56189414-AA50-44AF-961F-6D8098E91F8CQ30863609-621648EB-E1C7-4361-A72D-647AEB21B247Q33319299-997DA446-33C2-4E14-98EB-08D5D2358A2BQ33327478-96C56164-5019-42E2-90C7-6636E936066AQ33933426-B9AF4E88-C7A9-4C6B-AC16-C7C7BC791339Q34241725-6E3A96AE-2EC5-4872-A31E-E902C10B2516Q35690713-A3B58AF0-EAB0-4067-A925-70DB97CC9A00Q35889422-383092D2-8DCD-4FAF-BB6A-F2B7E93913ABQ36063687-10F7B6D5-B8C7-4A93-863F-57396AC3E972Q36431914-F4ACF432-EE99-4E33-B772-F7A048917F37Q36596289-C5C44B81-1EC1-4FAF-A43B-598D6F7FCA45Q36838770-F22FD1F3-D2A2-4351-B2DA-4230E856E1C8Q37034278-E699A95C-D3E7-4064-ACE3-18EA515493D7Q37599802-C07D3D0A-722D-4F6D-8014-3E733381347CQ37768044-27823BDA-0DFE-4792-B20D-32A7356BDB21Q37967350-8ABEAFA9-3929-44DD-A0ED-BFF41B92872CQ38014826-37533167-4276-4D01-A920-B0CF8D926AF4Q38061990-343635F9-1A4E-4380-B8CF-0A486114963CQ38061998-AF90C363-9727-400E-B012-52D282D702B9Q39068332-61B61E96-90C3-4191-B496-6C12F4A649AEQ39084617-C8ECD1DA-DEED-4EDD-99E8-A831ECDA2D35Q39385959-B4846A10-F2E5-4FFE-93D9-E745D77712F4Q40182215-B73DD3BC-54B5-44FD-98A8-DA30D69CEA68Q40203941-7B37B481-B333-4A3E-A132-9B7F5ABF363EQ41817034-AB3D42B1-94DF-49BE-8D13-6C16DAE58B2DQ42323966-0605E6ED-5318-4112-A966-29B0EC979503Q47294747-364272B1-47D2-436E-90CB-8363064A1DDCQ47609581-825FA04A-75F2-4642-B172-FD5A73017754Q50713990-15F16814-2749-40C0-8ACB-22024E0BC7C4Q57306381-6E7554C9-911D-40B4-A2B9-7B1DD1B71621
P2860
Multiple regions contribute to membrane targeting of Rab GTPases.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Multiple regions contribute to membrane targeting of Rab GTPases.
@en
type
label
Multiple regions contribute to membrane targeting of Rab GTPases.
@en
prefLabel
Multiple regions contribute to membrane targeting of Rab GTPases.
@en
P2093
P356
P1476
Multiple regions contribute to membrane targeting of Rab GTPases.
@en
P2093
Christina Wasmeier
Lynn Lamoreux
Molly Strom
P304
P356
10.1242/JCS.01542
P407
P577
2004-11-23T00:00:00Z