Structural characterization of the MIT domain from human Vps4b

Takasu, Hirotoshi; Jee, Jun Goo; Ohno, Ayako; Goda, Nobuhito; Fujiwara, Kazue; Tochio, Hidehito; Shirakawa, Masahiro; Hiroaki, Hidekazu

doi:10.1016/j.bbrc.2005.06.110

Cited by 34 publications

(35 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The nucleotide sequence predicted a protein of 435 amino acid residues and ;48.5 kD that is 54% identical and 67% similar to yeast Vps4p ( Figure 1A). The analysis of the predicted protein sequence indicated that, like yeast Vps4p and mammalian SKD1 (Fujita et al, 2004;Scott et al, 2005aScott et al, , 2005bTakasu et al, 2005), At-SKD1 has a modular structure, with an N-terminal region containing a microtubule interacting and trafficking domain, a canonical AAA ATPase cassette, and a C-terminal domain ( Figure 1A). …”

Section: Identification Of Skd1 Homologs In Arabidopsismentioning

confidence: 99%

TheArabidopsisAAA ATPase SKD1 Is Involved in Multivesicular Endosome Function and Interacts with Its Positive Regulator LYST-INTERACTING PROTEIN5

et al. 2007

View full text Add to dashboard Cite

In yeast and mammals, the AAA ATPase Vps4p/SKD1 (for Vacuolar protein sorting 4/SUPPRESSOR OF K þ TRANSPORT GROWTH DEFECT1) is required for the endosomal sorting of secretory and endocytic cargo. We identified a VPS4/SKD1 homolog in Arabidopsis thaliana, which localizes to the cytoplasm and to multivesicular endosomes. In addition, green fluorescent protein-SKD1 colocalizes on multivesicular bodies with fluorescent fusion protein endosomal Rab GTPases, such as ARA6/RabF1, RHA1/RabF2a, and ARA7/RabF2b, and with the endocytic marker FM4-64. The expression of SKD1 E232Q , an ATPase-deficient version of SKD1, induces alterations in the endosomal system of tobacco (Nicotiana tabacum) Bright Yellow 2 cells and ultimately leads to cell death. The inducible expression of SKD1 E232Q in Arabidopsis resulted in enlarged endosomes with a reduced number of internal vesicles. In a yeast two-hybrid screen using Arabidopsis SKD1 as bait, we isolated a putative homolog of mammalian LYST-INTERACTING PROTEIN5 (LIP5)/SKD1 BINDING PROTEIN1 and yeast Vta1p (for Vps twenty associated 1 protein). Arabidopsis LIP5 acts as a positive regulator of SKD1 by increasing fourfold to fivefold its in vitro ATPase activity. We isolated a knockout homozygous Arabidopsis mutant line with a T-DNA insertion in LIP5. lip5 plants are viable and show no phenotypic alterations under normal growth conditions, suggesting that basal SKD1 ATPase activity is sufficient for plant development and growth.

show abstract

Section: Identification Of Skd1 Homologs In Arabidopsismentioning

confidence: 99%

TheArabidopsisAAA ATPase SKD1 Is Involved in Multivesicular Endosome Function and Interacts with Its Positive Regulator LYST-INTERACTING PROTEIN5

et al. 2007

View full text Add to dashboard Cite

show abstract

“…One of the most characteristic features of the MIT domain is its unique hydrophobic core formed by conserved Ala residues, referred to as the "Ala zipper" (40,41). These are thus identified as the key residues for the MIT domain signature (Ala-Xaa 6 -Ala-Xaa 11 -Ala-Xaa 6 -Ala).…”

Section: Structural Prediction and Sequence Analysis Of Kp60-ntd-mentioning

confidence: 99%

A Common Substrate Recognition Mode Conserved between Katanin p60 and VPS4 Governs Microtubule Severing and Membrane Skeleton Reorganization

Iwaya

Kuwahara

Fujiwara

et al. 2010

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Katanin p60 (kp60), a microtubule-severing enzyme, plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner. We show that a single domain isolated from the N terminus of mouse katanin p60 (kp60-NTD) binds to tubulin. The solution structure of kp60-NTD was determined by NMR. Although their sequence similarities were as low as 20%, the structure of kp60-NTD revealed a striking similarity to those of the microtubule interacting and trafficking (MIT) domains, which adopt anti-parallel three-stranded helix bundle. In particular, the arrangement of helices 2 and 3 is well conserved between kp60-NTD and the MIT domain from Vps4, which is a homologous protein that promotes disassembly of the endosomal sorting complexes required for transport III membrane skeleton complex. Mutation studies revealed that the positively charged surface formed by helices 2 and 3 binds tubulin. This binding mode resembles the interaction between the MIT domain of Vps4 and Vps2/ CHMP1a, a component of endosomal sorting complexes required for transport III. Our results show that both the molecular architecture and the binding modes are conserved between two AAA-ATPases, kp60 and Vps4. A common mechanism is evolutionarily conserved between two distinct cellular events, one that drives microtubule severing and the other involving membrane skeletal reorganization. Microtubules (MTs)2 are polymers of ␣-and ␤-tubulin heterodimers. MTs exist as networks that dynamically and rapidly reorganize during different phases of the cell cycle. Spontaneous growth as well as shortening at the ends is indispensable for functional rearrangement. For example, they form the mitotic spindle during M phase, which mediates chromosome segregation during cell division based on the nature of dynamic rearrangement of MTs (reviewed in Refs. 1, 2). Many cellular events involving MTs are driven not only by autonomous polymerization and dissociation of tubulin but also by MT-severing enzymes. These enzymes disassemble the MTs to promote large changes in the cytoskeleton in an ATP-dependent manner (3).There are three known MT-severing enzymes, katanin, spastin, and fidgetin, all of which belong to type I AAA-ATPases (4 -7). Katanin was first identified from sea urchin cytosol (8) and consists of two subunits as follows: a 60-kDa catalytic subunit (kp60) containing a single AAA domain, and an 80-kDa regulatory subunit (kp80) (9, 10). Both the subunits are genetically conserved among many higher eukaryotes. Katanin localizes at the centrosomes in an MT-dependent manner (11), which is probably required for recycling and for the poleward flux of tubulin in the spindle by disassembling MTs at their minus ends (12, 13). kp60 homologs are also found in plants, insects, and nematodes but not in yeasts.kp60 has a common domain organization typical of a type I AAA-ATPase, which consists of an N-terminal substrate binding region followed by a single AAA domain at the C terminus. In general, AAA-ATPases are believed to act as protein unfol...

show abstract

“…The MIT domain has been predicted to end at amino acid 77 (7,8). Removing the complete linker region, from amino acid 78 to 118, resulted in loss of Vps4 activity (⌬78 -118GS, Fig.…”

Section: Journal Of Biological Chemistrymentioning

confidence: 99%

The Linker Region Plays a Regulatory Role in Assembly and Activity of the Vps4 AAA ATPase

Shestakova

Davies

Katzmann

et al. 2013

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Vps4 functions in eukaryotic cells in membrane fission reactions. Results: Mutational analysis suggests that the long linker region of Vps4 is not essential but regulates this ATPase. Conclusion:The binding to the substrate ESCRT-III drives formation of the active Vps4 complex. Significance: Understanding the mechanism of Vps4 function gives insights into protein trafficking, cytokinesis, and virus formation.

show abstract

Structural characterization of the MIT domain from human Vps4b

Cited by 34 publications

References 23 publications

TheArabidopsisAAA ATPase SKD1 Is Involved in Multivesicular Endosome Function and Interacts with Its Positive Regulator LYST-INTERACTING PROTEIN5

TheArabidopsisAAA ATPase SKD1 Is Involved in Multivesicular Endosome Function and Interacts with Its Positive Regulator LYST-INTERACTING PROTEIN5

A Common Substrate Recognition Mode Conserved between Katanin p60 and VPS4 Governs Microtubule Severing and Membrane Skeleton Reorganization

The Linker Region Plays a Regulatory Role in Assembly and Activity of the Vps4 AAA ATPase

Contact Info

Product

Resources

About