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Search results 301 to 307 out of 307 for Vps13b

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0.015s

Type

Details

Score

Protein

V9GX23

Organism:	Mus musculus/domesticus
Length:	3211
Fragment?:	true

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Publication

11381253 | -

First Author:	Rampoldi L
Year:	2001
Journal:	Nat Genet
Title:	A conserved sorting-associated protein is mutant in chorea-acanthocytosis.
Volume:	28
Issue:	2
Pages:	119-20

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Publication

30018089 | -

First Author:	Bean BDM
Year:	2018
Journal:	J Cell Biol
Title:	Competitive organelle-specific adaptors recruit Vps13 to membrane contact sites.
Volume:	217
Issue:	10
Pages:	3593-3607

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Publication

23444357 | -

First Author:	Koizumi K
Year:	2013
Journal:	Development
Title:	Identification of SHRUBBY, a SHORT-ROOT and SCARECROW interacting protein that controls root growth and radial patterning.
Volume:	140
Issue:	6
Pages:	1292-300

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Protein Domain

IPR009543 | VPS13_VAB

Type:

Domain

Description:

This entry represents the VPS13 adaptor binding (VAB) domain, previously known as SHR-BD, found in VPS13 [, ]. This domain interacts with Ypt35 which recruits VPS13 to endosomal and vacuolar membranes, and with Mcp1 to target VPS13 at mitochondria []. In plants, this domain is found to be the region which interacts with SHR or the SHORT-ROOT transcription factor, a regulator of root-growth and asymmetric cell division that separates ground tissue into endodermis and cortex. The plant protein containing the SHR-BD is named SHRUBBY or SHBY () []. This domain interacts with Proline-X-Proline (Pro-X-Pro) motif present in receptor proteins at contact sites [].This domain comprises six repeated modules, each of them containing nine ��-strands connected by loops and arranged into a ��-sandwich [].VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [, , ]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. Most evidence showed that mammalian VPS13A, VPS13C and VPS13D localize at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localize to endosome-endosome contacts [, , ]. Mutations in human VPS13 proteins (VPS13A-D) cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia, respectively which suggests they have different functions [, ]. Members of this entry belong to the repeating ��-groove (RBG) superfamily. These proteins share a structure made of multiple repeating modules consisting of five ��-sheets followed by a loop [].

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Publication

30709847 | -

First Author:	Mu?oz-Braceras S
Year:	2019
Journal:	Dis Model Mech
Title:	VPS13A is closely associated with mitochondria and is required for efficient lysosomal degradation.
Volume:	12
Issue:	2

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Publication

35491307 | -

First Author:	Neuman SD
Year:	2022
Journal:	Trends Cell Biol
Title:	A novel superfamily of bridge-like lipid transfer proteins.
Volume:	32
Issue:	11
Pages:	962-974

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