Structure of the VHS Domain of Human Tom1 (Target of Myb 1):  Insights into Interactions with Proteins and Membranes‡

Biochemistry ◽  
2000 ◽  
Vol 39 (37) ◽  
pp. 11282-11290 ◽  
Author(s):  
Saurav Misra ◽  
Bridgette M. Beach ◽  
James H. Hurley
Keyword(s):  
Vhs Domain

scholarly journals Insights into the Phosphoregulation of β-Secretase Sorting Signal by the VHS Domain of GGA1

Traffic ◽  
2004 ◽  
Vol 5 (6) ◽  
pp. 437-448 ◽  
Author(s):  
Tomoo Shiba ◽  
Satoshi Kametaka ◽  
Masato Kawasaki ◽  
Masahiro Shibata ◽  
Satoshi Waguri ◽  
...  
Keyword(s):  
Sorting Signal ◽  
Vhs Domain

VHS domain - a longshoreman of vesicle lines

FEBS Letters ◽  
2001 ◽  
Vol 513 (1) ◽  
pp. 19-23 ◽  
Author(s):  
Olli Lohi ◽  
Anssi Poussu ◽  
Yuxin Mao ◽  
Florante Quiocho ◽  
Veli-Pekka Lehto
Keyword(s):  
Vhs Domain

Backbone 1H, 15N, and 13C resonance assignments of the Tom1 VHS domain

2016 ◽  
Vol 11 (1) ◽  
pp. 1-4 ◽  
Author(s):  
Jeffrey F. Ellena ◽  
Wen Xiong ◽  
Xiaolin Zhao ◽  
Narasimhamurthy Shanaiah ◽  
Daniel G. S. Capelluto
Keyword(s):  
Resonance Assignments ◽  
Vhs Domain

Phosphoregulation of sorting signal–VHS domain interactions by a direct electrostatic mechanism

2002 ◽  
Author(s):  
Yukio Kato ◽  
Saurav Misra ◽  
Rosa Puertollano ◽  
James H. Hurley ◽  
Juan S. Bonifacino
Keyword(s):  
Sorting Signal ◽  
Domain Interactions ◽  
Vhs Domain ◽  
Electrostatic Mechanism

Letter to the Editor: NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from Arabidopsis thaliana

2004 ◽  
Vol 29 (2) ◽  
pp. 205-206 ◽  
Author(s):  
Blanca López-Méndez ◽  
David Pantoja-Uceda ◽  
Tadashi Tomizawa ◽  
Seizo Koshiba ◽  
Takanori Kigawa ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Nmr Assignment ◽  
Letter To The Editor ◽  
Vhs Domain

scholarly journals The Vps27/Hrs/STAM (VHS) Domain of the Signal-transducing Adaptor Molecule (STAM) Directs Associated Molecule with the SH3 Domain of STAM (AMSH) Specificity to Longer Ubiquitin Chains and Dictates the Position of Cleavage

2015 ◽  
Vol 291 (4) ◽  
pp. 2033-2042 ◽  
Author(s):  
Nardeen Baiady ◽  
Prasanth Padala ◽  
Bayan Mashahreh ◽  
Einav Cohen-Kfir ◽  
Emily A. Todd ◽  
...  
Keyword(s):  
Structural Model ◽  
Sh3 Domain ◽  
Deubiquitinating Enzyme ◽  
Cleavage Rate ◽  
Ubiquitin Chain ◽  
Interacting Protein ◽  
Chain Cleavage ◽  
Substrate Cleavage ◽  
Vhs Domain

The deubiquitinating enzyme associated molecule with the SH3 domain of STAM (AMSH) is crucial for the removal of ubiquitin molecules during receptor-mediated endocytosis and lysosomal receptor sorting. AMSH interacts with signal transducing adapter molecule (STAM) 1 or 2, which enhances the activity of AMSH through an unknown mechanism. This stimulation is dependent on the ubiquitin-interacting motif of STAM. Here we investigate the specific mechanism of AMSH stimulation by STAM proteins and the role of the STAM Vps27/Hrs/STAM domain. We show that, in the presence of STAM, the length of the ubiquitin chains affects the apparent cleavage rate. Through measurement of the chain cleavage kinetics, we found that, although the kcat of Lys63-linked ubiquitin chain cleavage was comparable for di- and tri-ubiquitin, the Km value was lower for tri-ubiquitin. This increased affinity for longer chains was dependent on the Vps27/Hrs/STAM domain of STAM and required that the substrate ubiquitin chain contain homogenous Lys63-linkages. In addition, STAM directed AMSH cleavage toward the distal isopeptide bond in tri-ubiquitin chains. Finally, we generated a structural model of AMSH-STAM to show how the complex binds Lys63-linked ubiquitin chains and cleaves at the distal end. These data show how a deubiquitinating enzyme-interacting protein dictates the efficiency and specificity of substrate cleavage.

The Emerging Role of VHS Domain-Containing Tom1, Tom1L1 and Tom1L2 in Membrane Trafficking

Traffic ◽  
2010 ◽  
Vol 11 (9) ◽  
pp. 1119-1128 ◽  
Author(s):  
Tuanlao Wang ◽  
Ning Sheng Liu ◽  
Li-Fong Seet ◽  
Wanjin Hong
Keyword(s):  
Membrane Trafficking ◽  
Vhs Domain

scholarly journals Direct binding of the Kex2p cytosolic tail to the VHS domain of yeast Gga2p facilitates TGN to prevacuolar compartment transport and is regulated by phosphorylation

2013 ◽  
Vol 24 (4) ◽  
pp. 495-509 ◽  
Author(s):  
Mithu De ◽  
Mohamed E. Abazeed ◽  
Robert S. Fuller
Keyword(s):  
Glutathione S Transferase ◽  
Sorting Signals ◽  
Biochemical Assays ◽  
Direct Binding ◽  
Prevacuolar Compartment ◽  
Vhs Domain ◽  
A Site ◽  
Golgi Network ◽  
Adp Ribosylation Factor

Human Golgi-localized, γ-ear–containing, ADP-ribosylation factor–binding proteins (Ggas) bind directly to acidic dileucine sorting motifs in the cytosolic tails (C-tails) of intracellular receptors. Despite evidence for a role in recruiting ubiquitinated cargo, it remains unclear whether yeast Ggas also function by binding peptide-sorting signals directly. Two-hybrid analysis shows that the Gga1p and Gga2p Vps27, Hrs, Stam (VHS) domains both bind a site in the Kex2p C-tail and that the Gga2p VHS domain binds a site in the Vps10p C-tail. Binding requires deletion of an apparently autoinhibitory sequence in the Gga2p hinge. Ser780in the Kex2p C-tail is crucial for binding: an Ala substitution blocks but an Asp substitution permits binding. Biochemical assays using purified Gga2p VHS–GGA and TOM1 (GAT) and glutathione S-transferase–Kex2p C-tail fusions show that Gga2p binds directly to the Kex2p C-tail, with relative affinities Asp780> Ser780> Ala780. Affinity-purified antibody against a peptide containing phospho-Ser­780recognizes wild-type Kex2p but not S780A Kex2p, showing that Ser780is phosphorylated in vivo; phosphorylation of Ser780is up-regulated by cell wall–damaging drugs. Finally, mutation of Ser780alters trafficking of Kex2p both in vivo and in cell-free trans-Golgi network (TGN)–prevacuolar compartment (PVC) transport. Thus yeast Gga adaptors facilitate TGN–PVC transport by direct binding of noncanonical phosphoregulated Gga-binding sites in cargo molecules.

scholarly journals Preferential phosphatidylinositol 5-phosphate binding contributes to a destabilization of the VHS domain structure of Tom1

2019 ◽  
Author(s):  
Wen Xiong ◽  
Tuo-Xian Tang ◽  
Evan Littleton ◽  
Arba Karcini ◽  
Iulia M. Lazar ◽  
...  
Keyword(s):  
Domain Structure ◽  
Isothermal Calorimetry ◽  
Shigella Flexneri ◽  
Protein Domain ◽  
Bacterial Survival ◽  
Phosphate Binding ◽  
Reducing Conditions ◽  
Relevant Role ◽  
Vhs Domain ◽  
And Function

AbstractTom1 transports endosomal ubiquitinated proteins that are targeted for degradation in the lysosomal pathway. Infection of eukaryotic cells by Shigella flexneri boosts oxygen consumption and promotes the synthesis of phosphatidylinositol-5-phosphate [PtdIns5P], which triggers Tom1 translocation to signaling endosomes. Removing Tom1 from its cargo trafficking function hinders protein degradation in the host and, simultaneously, enables bacterial survival. Tom1 preferentially binds PtdIns5P via its VHS domain, but the effects of a reducing environment as well as PtdIns5P on the domain structure and function are unknown. Thermal denaturation studies demonstrate that, under reducing conditions, the monomeric Tom1 VHS domain switches from a three-state to a two-state transition behavior. PtdIns5P reduced thermostability, interhelical contacts, and conformational compaction of Tom1 VHS, suggesting that the phosphoinositide destabilizes the protein domain. Destabilization of Tom1 VHS structure was also observed with other phospholipids. Isothermal calorimetry data analysis indicates that, unlike ubiquitin, Tom1 VHS endothermically binds to PtdIns5P through two noncooperative binding sites, with its acyl chains playing a relevant role in the interaction. Altogether, these findings provide mechanistic insights about the recognition of PtdIns5P by the VHS domain that may explain how Tom1, when in a different VHS domain conformational state, interacts with downstream effectors under S. flexneri infection.

scholarly journals Golgi-Localized, γ-Ear-Containing, Arf-Binding Protein Adaptors Mediate Insulin-Responsive Trafficking of Glucose Transporter 4 in 3T3-L1 Adipocytes

2005 ◽  
Vol 19 (8) ◽  
pp. 2145-2153 ◽  
Author(s):  
Lin V. Li ◽  
Konstantin V. Kandror
Keyword(s):  
Glucose Transporter ◽  
Adaptor Proteins ◽  
Dominant Negative ◽  
Glucose Transporter 4 ◽  
Glutathione S Transferase ◽  
Insulin Responsiveness ◽  
Vhs Domain

Abstract Small glucose transporter 4 (Glut4)-containing vesicles represent the major insulin-responsive compartment in fat and skeletal muscle cells. The molecular mechanism of their biogenesis is not yet elucidated. Here, we studied the role of the newly discovered family of monomeric adaptor proteins, GGA (Golgi-localized, γ-ear-containing, Arf-binding proteins), in the formation of small Glut4 vesicles and acquisition of insulin responsiveness in 3T3-L1 adipocytes. In these cells, all three GGA isoforms are expressed throughout the differentiation process. In particular, GGA2 is primarily present in trans-Golgi network and endosomes where it demonstrates a significant colocalization with the recycling pool of Glut4. Using the techniques of immunoadsorption as well as glutathione-S-transferase pull-down assay we found that Glut4 vesicles (but not Glut4 per se) interact with GGA via the Vps-27, Hrs, and STAM (VHS) domain. Moreover, a dominant negative GGA mutant inhibits formation of Glut4 vesicles in vitro. To study a possible role of GGA in Glut4 traffic in the living cell, we stably expressed a dominant negative GGA mutant in 3T3-L1 adipocytes. Formation of small insulin-responsive Glut4-containing vesicles and insulin-stimulated glucose uptake in these cells were markedly impaired. Thus, GGA adaptors participate in the formation of the insulin-responsive vesicular compartment from the intracellular donor membranes both in vivo and in vitro.

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