A Novel Mechanism of Regulating the ATPase VPS4 by Its Cofactor LIP5 and the Endosomal Sorting Complex Required for Transport (ESCRT)-III Protein CHMP5

Vild, C.J.; Li, Yan; Guo, E.Z.; Liu, Yuan; Xu, Zhaohui

doi:10.1074/jbc.m114.616730

Cited by 29 publications

(44 citation statements)

References 54 publications

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“…Consistent with its central role in the ESCRT pathway, its activity is controlled by multiple mechanisms. Vta1p/LIP5 increases in vitro Vps4p/SKD1 ATPase activity in yeast, animals, and plants (Lottridge et al, 2006;Haas et al, 2007;Vild et al, 2015). In yeast, the C-terminal domain of Vta1p binds to Vps4p, enhancing its oligomerization (Azmi et al, 2006;Lottridge et al, 2006;Yang and Hurley, 2010;Norgan et al, 2013;Davies et al, 2014).…”

mentioning

confidence: 99%

“…Besides the direct activation of SKD1/Vps4p by LIP5/Vta1p, the core ESCRT-III proteins help recruit and activate the Vps4p/SKD1 ATPase complex (Saksena et al, 2009;Davies et al, 2010) by substrate engagement. Finally, the ESCRT-III accessory subunits Did2p/CHMP1, Vps60p/CHMP5, and IST1 also aid in the recruitment of Vps4p/SKD1 to the endosomal membrane and interact directly with Vta1p/LIP5 (Azmi et al, 2008;Dimaano et al, 2008;Agromayor et al, 2009;Bajorek et al, 2009;Vild et al, 2015).…”

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confidence: 99%

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Role of SKD1 Regulators LIP5 and IST1-LIKE1 in Endosomal Sorting and Plant Development

et al. 2016

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SKD1 is a core component of the mechanism that degrades plasma membrane proteins via the Endosomal Sorting Complex Required for Transport (ESCRT) pathway. Its ATPase activity and endosomal recruitment are regulated by the ESCRT components LIP5 and IST1. How LIP5 and IST1 affect ESCRT-mediated endosomal trafficking and development in plants is not known. Here we use Arabidopsis mutants to demonstrate that LIP5 controls the constitutive degradation of plasma membrane proteins and the formation of endosomal intraluminal vesicles. Although lip5 mutants were able to polarize the auxin efflux facilitators PIN2 and PIN3, both proteins were mis-sorted to the tonoplast in lip5 root cells. In addition, lip5 root cells over-accumulated PIN2 at the plasma membrane. Consistently with the trafficking defects of PIN proteins, the lip5 roots showed abnormal gravitropism with an enhanced response within the first 4 h after gravistimulation. LIP5 physically interacts with IST1-LIKE1 (ISTL1), a protein predicted to be the Arabidopsis homolog of yeast IST1. However, we found that Arabidopsis contains 12 genes coding for predicted IST1-domain containing proteins (ISTL1-12). Within the ISTL1-6 group, ISTL1 showed the strongest interaction with LIP5, SKD1, and the ESCRT-III-related proteins CHMP1A in yeast two hybrid assays. Through the analysis of single and double mutants, we found that the synthetic interaction of LIP5 with ISTL1, but not with ISTL2, 3, or 6, is essential for normal plant growth, repression of spontaneous cell death, and post-embryonic lethality.

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confidence: 99%

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confidence: 99%

Role of SKD1 Regulators LIP5 and IST1-LIKE1 in Endosomal Sorting and Plant Development

et al. 2016

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“…The complex Vta1NTD- Did2 176–204 structure shows that the bound Vta1NTD still has two MIT domains, each of them is composed of three α-helices (MIT1: helices α1, α2 and α3; MIT2: helices α5, α6 and α7; respectively), almost similar to those observed in its free state and in its complex with Vps60 128–186 2933343536. The backbone atoms belonging to MIT1 and MIT2 regions of bound Vta1NTD have RMSD values of 1.7 Å and 1.8 Å with those of free Vta1NTD (Fig.…”

Section: Resultsmentioning

confidence: 53%

“…The bound Did2 176–204 adopts an overall rod-like helix structure with a flexible loop in its N-terminus (similar to free Did2 176–204 with an RMSD value of 0.5 Å for the backbone atoms in secondary structure region). The helix consists of residues 187′–203′, a little longer than that (residues 184′–198′) observed in LIP5NTD-CHIMP1B complex structure36. The Did2 176–204 α-helix sits on the surface groove formed by the 2 nd and the 3 rd helices of Vta1NTD MIT1 in a mode similar to that observed in Vps4-CHMP1A complex structure20 and that observed in human LIP5NTD-CHMP1B and LIP5NTD-CHMP1B-CHMP5 complex structures36.…”

Section: Resultsmentioning

confidence: 58%

“…Our NMR structural studies on the interactions between Vta1NTD and Vps60 128–186 revealed that Vps60 128–186 interacted with Vta1NTD in a novel MIT recognition mode, i.e. , through its helices α4′ and α5′ extending over helices 5, 6 and 7 of Vta1NTD MIT2 domain33343536. Previous studies indicated that the C-terminal of Did2, residues 176–204, named as Did2 176–204 in this whole report, as shown in Fig.…”

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confidence: 57%

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NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway

Shen

Yang

Wang

et al. 2016

Sci Rep

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As an AAA-ATPase, Vps4 is important for function of multivesicular bodies (MVB) sorting pathway, which involves in cellular phenomena ranging from receptor down-regulation to viral budding to cytokinesis. The activity of Vps4 is stimulated by the interactions between Vta1 N-terminus (named as Vta1NTD) and Did2 fragment (176–204 aa) (termed as Did2176–204) or Vps60 (128–186 aa) (termed as Vps60128–186). The structural basis of how Vta1NTD binds to Did2176–204 is still unclear. To address this, in this report, the structure of Did2176–204 in complex with Vta1NTD was determined by NMR techniques, demonstrating that Did2176–204 interacts with Vta1NTD through its helix α6′ extending over the 2nd and the 3rd α-helices of Vta1NTD microtubule interacting and transport 1 (MIT1) domain. The residues within Did2176–204 helix α6′ in the interface make up of an amino acid sequence as E192′xxL195′xxR198′L199′xxL202′R203′, identical to type 1 MIT-interacting motif (MIM1) (D/E)xxLxxRLxxL(K/R) of CHMP1A180–196 observed in Vps4-CHMP1A complex structure, indicating that Did2 binds to Vta1NTD through canonical MIM1 interactions. Moreover, the Did2 binding does not result in Vta1NTD significant conformational changes, revealing that Did2, similar to Vps60, enhances Vta1 stimulation of Vps4 ATPase activity in an indirect manner.

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VPS4B deficiency causes early embryonic lethality and induces signal transduction disorders of cell endocytosis

Chen

Lü

et al. 2021

Genesis

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Summary VPS4B (vacuolar protein sorting 4B), a member of the ATPase associated with diverse cellular activities (AAA) protein family, is a component of the endosomal sorting complexes required for transport machinery which regulates the internalization and lysosomal degradation of membrane proteins. We previously reported that VPS4B is one of the pathogenic genes related to dentin dysplasia type I, although its function was largely unknown. To investigate the role of VPS4B in tooth development, we deleted the Vps4b gene in mice. We found that heterozygous knockout mice (Vps4b+/−) developed normally and were fertile. However, homozygous deletion of the Vps4b gene resulted in early embryonic lethality of Vps4b−/− mice at approximately embryonic day 9.5 (E9.5). To investigate the underlying molecular mechanisms, we examined the molecular functions of VPS4B in vivo and in vitro. Cell experiments showed that VPS4B influenced the proliferation, apoptosis, and cell cycle of transfected human neuroblastoma cells (IMR‐32 cells) with over‐expression or knockdown of VPS4B. Moreover, qRT‐PCR detection showed that the mRNA expression levels of apoptosis‐, cell cycle‐, and endocytosis‐related genes was significantly down or up‐regulated in RNA interference‐mediated knockdown of VPS4B in IMR‐32 cells and Vps4b+/− E12.5 embryos. We accordingly speculated that signal transduction disorders of cell endocytosis are a contributing factor to the prenatal lethality of Vps4b−/− mice.

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A Novel Mechanism of Regulating the ATPase VPS4 by Its Cofactor LIP5 and the Endosomal Sorting Complex Required for Transport (ESCRT)-III Protein CHMP5

Cited by 29 publications

References 54 publications

Role of SKD1 Regulators LIP5 and IST1-LIKE1 in Endosomal Sorting and Plant Development

Role of SKD1 Regulators LIP5 and IST1-LIKE1 in Endosomal Sorting and Plant Development

NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway

VPS4B deficiency causes early embryonic lethality and induces signal transduction disorders of cell endocytosis

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