VTA1

Last update 08 May 2025

Basic Info

Synonyms

C6orf55, Dopamine-responsive gene 1 protein, DRG-1

+ [9]

Introduction

Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR (By similarity). Involved in HIV-1 budding.

100 Clinical Results associated with VTA1

100 Translational Medicine associated with VTA1

0 Patents (Medical) associated with VTA1

Literatures (Medical) associated with VTA1

15 Apr 2025·Journal of Virology

Coordination of the host Vps4-Vta1 complex and the viral core protein Ac93 facilitates entry of Autographa californica multiple nucleopolyhedrovirus budded virions

Article

Author: Yue, Xiaorong ; Li, Zhaofei ; Ji, Ning ; Bai, Lisha ; Yu, Qianlong ; Ma, Yixiang

ABSTRACT The endosomal sorting complex required for transport (ESCRT) is a protein machine mediating membrane scission. In intraluminal vesicle (ILV) formation, ESCRT-0 targets cargoes and recruits ESCRT-I/-II to create membrane invagination, whereas ESCRT-III coordinates with the AAA ATPase Vps4 and its cofactor Vta1 to catalyze the membrane fission. Recently, ESCRT-I/-III and Vps4 were found to be involved in the entry of the baculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV). However, the necessity of other ESCRT components and the interplay of viral proteins and ESCRTs in regulating the virus entry remain elusive. Here, we identified ESCRT-0 (Hse1 and Vps27), ESCRT-II (Vps22, Vps25, and Vps36), and Vta1 of Spodoptera frugiperda . RNAi depletion of Vta1 but not the components of ESCRT-0 or ESCRT-II in Sf9 cells significantly reduced budded virus (BV) production. Quantitative PCR together with confocal microscopy analyses indicated that Vta1 was required for internalization and endosomal trafficking of BV. In the late phase of infection, although Vps4 and Vta1 were both distributed to the nucleus and at the plasma membrane, depletion of Vta1 did not affect BV release. Further analysis revealed that 7 of 14 BV envelope proteins (Ac75, Ac93, E25, F-like, P33, P48, and vUbiquitin) interacted with Vps4 and Vta1. Intriguingly, Ac93 adopted a similar mode as ESCRT-III proteins to interact with the microtubule-interacting and transport (MIT) domains of Vps4 and Vta1 via its C-terminal MIT-interacting motifs (MIM1), and the interactions were necessary for BV internalization. Together, our studies highlight the coordination of Vps4-Vta1 and Ac93, and probably other BV envelope proteins, in facilitating entry of AcMNPV. IMPORTANCEThe endosomal sorting complex required for transport (ESCRT) system is involved in the entry of diverse DNA and RNA viruses. However, the interplay of viral proteins and ESCRTs in promoting virus endocytosis remains largely unknown. Here, we found that the ESCRT early acting factors ESCRT-0/-II were not necessary for infectious budded virus (BV) production of Autographa californica multiple nucleopolyhedrovirus (AcMNPV). In contrast, the Vps4 cofactor Vta1 was required for entry but not egress of BV. Several core or essential BV envelope proteins were identified to interact with Vps4 and Vta1. Among them, Ac93 plays a central role in connecting other viral proteins and mimics ESCRT-III proteins to interact with Vps4-Vta1, facilitating entry of BV virions. These studies provide evidence for the coordination of viral proteins and ESCRTs in regulating entry of large enveloped DNA viruses.

07 Feb 2025·Plant Physiology

The ASPARAGINE-RICH PROTEIN–LYST-INTERACTING PROTEIN5 complex regulates noncanonical AUTOPHAGY8 degradation in Arabidopsis

Article

Author: Wu, Yanying ; Zheng, Danni ; Kong, Jiaxin ; Zhu, Kaikai ; Zhou, Weihong ; Tian, Wenqi ; Li, Jiajia ; Wang, Xue ; Xing, Enzhen ; Chen, Si ; Liu, Xinqi ; Gao, Ming ; Men, Shuzhen

AbstractThe endocytic and autophagic pathways play important roles in abiotic stress responses and maintaining cellular homeostasis in plants. Asparagine-rich proteins (NRPs) are plant-specific, stress-responsive proteins that are involved in many abiotic stress-related signaling pathways. We previously demonstrated that NRP promotes PIN FORMED 2 (PIN2) vacuolar degradation to maintain PIN2 homeostasis under abscisic acid treatment in Arabidopsis (Arabidopsis thaliana). However, the molecular function and mechanism of NRP in cellular vesicle trafficking remain unknown. In this study, we report that NRP directly interacts with LIP5 and ATG8, critical components of the endocytic and autophagic pathways, respectively. Genetic analyses show that NRP overexpression rescues canonical autophagy defects in a LIP5-dependent manner. Cellular and biochemical evidence indicates that NRP–LIP5 recruits ATG8 to multivesicular bodies for further vacuolar degradation, implying that a novel NRP-mediated endocytic pathway is utilized to compensate for the canonical autophagy defects that occur during plant stress responses. These findings provide insights into the crosstalk between the endocytic and autophagic pathways and uncover a function of ATG8 distinct from its canonical role in autophagy. The mechanism revealed here confers an evolutionary advantage to plants and provides a molecular basis for breeding crops with greater stress tolerance.

01 Jun 2023·Mycoses

Differential lipase virulence in Malassezia furfur dimorphism isolated from pityriasis versicolor patients and healthy individuals

Article

Author: Laliam, Angkana ; Nosanchuk, Joshua D. ; Pruksaphon, Kritsada ; Youngchim, Sirida ; Chaicumpar, Kunyaluk ; Thammasit, Patcharin

AbstractBackgroundMalassezia furfur is a member of the human skin microbiomes that can cause various skin diseases. Dimorphism plays a role as the yeast phase predominates during skin colonisation whereas mycelial forms are observed in the scales of patients with pityriasis versicolor (PV). However, due to their condition‐dependence for growth, it is difficult to culture M. furfur and this is an additional challenge for studying the pathogenicity of this fungus.ObjectiveTo describe different media suitable for culturing Malassezia from the yeast phase into mycelial forms, with a particular focus on nutritional supplements and pH conditions.MethodsClinical M. furfur isolates from patients with PV and healthy individuals were used to investigate Malassezia dimorphism as well as the activity and expression of lipase enzymes.ResultsOur experimental media were significantly more likely to promote mycelial growth in strains from healthy individuals compared to those from patients with PV. Lipase activity was increased in the mycelial phase cells compared to yeast forms for all strains tested. Assessment of the relative transcriptional expression of lipase within M. furfur revealed that LIP‐coding genes were upregulated in mycelium relative to yeast forms for the strains tested. However, the increases in LIP3, LIP5 and LIP6 gene expressions were significantly greater in strains from healthy individuals compared to those from patients with PV.ConclusionOverall, this study validated effective growth conditions to study M. furfur virulence factors and demonstrated that lipase is associated with M. furfur dimorphism.

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VTA1

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