Targeted mutation of the MLN64 START domain causes only modest alterations in cellular sterol metabolism (Q28245167)

GOA release 2020-03-11

author name string

Tatsuro Kishida

1

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Igor Kostetskii

2

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Zhibing Zhang

3

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Federico Martinez

4

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Pei Liu

5

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Steven U Walkley

6

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Nancy K Dwyer

7

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E Joan Blanchette-Mackie

8

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Glenn L Radice

9

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Jerome F Strauss

Journal of Biological Chemistry

10

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language of work or name

English

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publication date

30 April 2004

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published in

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volume

279

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issue

18

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page(s)

19276-85

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cites work

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The cholesterol-regulated StarD4 gene encodes a StAR-related lipid transfer protein with two closely related homologues, StarD5 and StarD6

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Steroidogenic acute regulatory protein (StAR) is a sterol transfer protein

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Role of steroidogenic acute regulatory protein in adrenal and gonadal steroidogenesis

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Targeted disruption of the mouse gene encoding steroidogenic acute regulatory protein provides insights into congenital lipoid adrenal hyperplasia

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START: a lipid-binding domain in StAR, HD-ZIP and signalling proteins

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Structure and lipid transport mechanism of a StAR-related domain

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Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain

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MLN64 exhibits homology with the steroidogenic acute regulatory protein (STAR) and is over-expressed in human breast carcinomas

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MLN64 contains a domain with homology to the steroidogenic acute regulatory protein (StAR) that stimulates steroidogenesis

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MLN64 mediates mobilization of lysosomal cholesterol to steroidogenic mitochondria

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The steroidogenic acute regulatory protein homolog MLN64, a late endosomal cholesterol-binding protein.

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Identification of HE1 as the second gene of Niemann-Pick C disease

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Cholesterol overload promotes morphogenesis of a Niemann-Pick C (NPC)-like compartment independent of inhibition of NPC1 or HE1/NPC2 function

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Niemann-pick type C1 (NPC1) overexpression alters cellular cholesterol homeostasis

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Cholesterol accumulates in cell bodies, but is decreased in distal axons, of Niemann-Pick C1-deficient neurons

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Trafficking of cholesterol from cell bodies to distal axons in Niemann Pick C1-deficient neurons

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The Niemann-Pick C1 protein resides in a vesicular compartment linked to retrograde transport of multiple lysosomal cargo

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Spectrophotometric determination of phosphate esters in the presence and absence of orthophosphate

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Neurons in Niemann-Pick disease type C accumulate gangliosides as well as unesterified cholesterol and undergo dendritic and axonal alterations

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Interaction of hormone-sensitive lipase with steroidogenic acute regulatory protein: facilitation of cholesterol transfer in adrenal

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Transport of plasma membrane-derived cholesterol and the function of Niemann-Pick C1 Protein

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MENTHO, a MLN64 homologue devoid of the START domain

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Mice without phosphatidylcholine transfer protein have no defects in the secretion of phosphatidylcholine into bile or into lung airspaces

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Fate of Endogenously Synthesized Cholesterol in Niemann-Pick Type C1 Cells

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Identifiers

DOI

10.1074/JBC.M400717200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

14963026

1 reference

Consolidated OpenCitations Corpus – April 2017