ATPase and GTPase Tangos Drive Intracellular Protein Transport

scientific article published on 19 September 2016

ATPase and GTPase Tangos Drive Intracellular Protein Transport is …
instance of (P31):
review articleQ7318358
scholarly articleQ13442814

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P356DOI10.1016/J.TIBS.2016.08.012
P932PMC publication ID5627767
P698PubMed publication ID27658684

P2093author name stringShu-Ou Shan
P2860cites workA cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutantsQ24339624
The 'invisible hand': regulation of RHO GTPases by RHOGDIsQ24606819
Mechanism of association and reciprocal activation of two GTPasesQ24793044
Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDPQ27619221
Crystal structure of the ribonucleoprotein core of the signal recognition particleQ27621449
The conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPaseQ27634944
Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptorQ27640772
X-ray structure of the T. Aquaticus Ftsy:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPasesQ27640901
Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communicationQ27642709
Substrate twinning activates the signal recognition particle and its receptorQ27642945
Heterodimeric GTPase Core of the SRP Targeting ComplexQ27642961
The structural basis of tail-anchored membrane protein recognition by Get3Q27656979
Model for eukaryotic tail-anchored protein binding based on the structure of Get3Q27657172
Structural insights into tail-anchored protein binding and membrane insertion by Get3Q27658386
Recognition of a signal peptide by the signal recognition particleQ27660413
Invited review: Small GTPases and their GAPsQ38772657
Invited review: Activation of G proteins by GTP and the mechanism of Gα-catalyzed GTP hydrolysisQ38782431
The mechanism of tail-anchored protein insertion into the ER membraneQ39502102
Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargoQ40031008
Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activityQ40387036
Signal sequence recognition and protein targeting to the endoplasmic reticulum membraneQ40611469
Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptorQ41738801
Ribosome binding induces repositioning of the signal recognition particle receptor on the transloconQ41867811
Signal sequences activate the catalytic switch of SRP RNA.Q41890905
Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA.Q42019821
Sequential checkpoints govern substrate selection during cotranslational protein targetingQ42235192
Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA.Q42530388
Synergistic actions between the SRP RNA and translating ribosome allow efficient delivery of the correct cargos during cotranslational protein targetingQ42718523
Role of SRP RNA in the GTPase cycles of Ffh and FtsY.Q43817010
Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPasesQ46341937
The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domainsQ46913511
SIMIBI twins in protein targeting and localizationQ47742493
Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP.Q50514376
Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix.Q54435413
Interaction of Guanine Nucleotides with the Signal Recognition Particle fromEscherichia coli†Q58237112
The arginine finger strikes againQ59081078
Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptorQ27666368
Structural basis of signal-sequence recognition by the signal recognition particleQ27666759
The Crystal Structure of the Signal Recognition Particle in Complex with Its ReceptorQ27666996
Structural Basis for Tail-Anchored Membrane Protein Biogenesis by the Get3-Receptor ComplexQ27670623
The mechanism of membrane-associated steps in tail-anchored protein insertionQ27671975
The Structural Basis of FtsY Recruitment and GTPase Activation by SRP RNAQ27680567
Crystal structure of ATP-bound Get3–Get4–Get5 complex reveals regulation of Get3 by Get4Q27683285
Structure of the conserved GTPase domain of the signal recognition particleQ27734632
Crystal structure of the NG domain from the signal-recognition particle receptor FtsYQ27734636
The GTPase superfamily: conserved structure and molecular mechanismQ27860524
A Chaperone Cascade Sorts Proteins for Posttranslational Membrane Insertion into the Endoplasmic ReticulumQ27931629
The GET complex mediates insertion of tail-anchored proteins into the ER membraneQ27932687
Identification of a targeting factor for posttranslational membrane protein insertion into the ERQ28294726
GEFs and GAPs: critical elements in the control of small G proteinsQ28304540
G proteins: transducers of receptor-generated signalsQ29547519
Classification and evolution of P-loop GTPases and related ATPasesQ29547655
Direct visualization reveals dynamics of a transient intermediate during protein assemblyQ30499803
Activated GTPase movement on an RNA scaffold drives co-translational protein targetingQ30530761
Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targetingQ33731247
Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targetingQ34083157
Differential gradients of interaction affinities drive efficient targeting and recycling in the GET pathwayQ34581057
The Get1/2 transmembrane complex is an endoplasmic-reticulum membrane protein insertaseQ35127549
Regulation by a chaperone improves substrate selectivity during cotranslational protein targetingQ35795958
Translation elongation regulates substrate selection by the signal recognition particleQ35801999
Signal recognition particles in chloroplasts, bacteria, yeast and mammals (review).Q36224486
Mechanism of Assembly of a Substrate Transfer Complex during Tail-anchored Protein TargetingQ36444249
Rab GTPase localization and Rab cascades in Golgi transportQ36458562
SecYEG activates GTPases to drive the completion of cotranslational protein targetingQ36618916
Precise timing of ATPase activation drives targeting of tail-anchored proteinsQ36835510
Multiple conformational switches in a GTPase complex control co-translational protein targetingQ37100829
Tail-anchored membrane protein insertion into the endoplasmic reticulumQ37140792
Molecular mechanism of GTPase activation at the signal recognition particle (SRP) RNA distal endQ37404996
It takes two to tango: regulation of G proteins by dimerizationQ37474358
Signal recognition particle: an essential protein-targeting machineQ38081948
Fidelity of cotranslational protein targeting by the signal recognition particleQ38217500
P433issue12
P1104number of pages11
P304page(s)1050-1060
P577publication date2016-09-19
P1433published inTrends in Biochemical SciencesQ1565711
P1476titleATPase and GTPase Tangos Drive Intracellular Protein Transport
P478volume41

Reverse relations

cites work (P2860)
Q90182677A molecular recognition feature mediates ribosome-induced SRP-receptor assembly during protein targeting
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Q91700786GTP hydrolysis promotes disassembly of the atlastin crossover dimer during ER fusion
Q90424090Guiding tail-anchored membrane proteins to the endoplasmic reticulum in a chaperone cascade
Q47620086Intersubunit Crosstalk in the Rag GTPase Heterodimer Enables mTORC1 to Respond Rapidly to Amino Acid Availability
Q55264962The ERA-Related GTPase AtERG2 Associated with Mitochondria 18S RNA Is Essential for Early Embryo Development in Arabidopsis.