Vesicular and Non-vesicular Sterol Transport in Living Cells

Hao, Mingming; Lin, Sharron X.; Karylowski, Ola; Wüstner, Daniel; McGraw, Timothy E.; Maxfield, Frederick R.

doi:10.1074/jbc.m108861200

Cited by 276 publications

(118 citation statements)

References 77 publications

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“…While some cholesterol transport is vesicular, cytosolic protein carriers have been proposed for other transport events, such as movement of newly synthesized cholesterol to the plasma membrane (3) and plasma membrane cholesterol to the endocytic recycling compartment (18). A START protein could also mediate sterol transport to mitochondrial sterol 27-hydroxylase (Cyp27) (19).…”

Section: Discussionmentioning

confidence: 99%

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

Soccio

Adams

Romanowski

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

174

162

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Using cDNA microarrays, we identified StarD4 as a gene whose expression decreased more than 2-fold in the livers of mice fed a high-cholesterol diet. StarD4 expression in cultured 3T3 cells was also sterol-regulated, and known sterol regulatory element binding protein (SREBP)-target genes showed coordinate regulation. The closest homologues to StarD4 were two other StAR-related lipid transfer (START) proteins named StarD5 and StarD6. StarD4, StarD5, and StarD6 are 205-to 233-aa proteins consisting almost entirely of START domains. These three constitute a subfamily among START proteins, sharing Ϸ30% amino acid identity with one another, Ϸ20% identity with the cholesterol-binding START domains of StAR and MLN64, and less than 15% identity with phosphatidylcholine transfer protein (PCTP) and other START domains. StarD4 and StarD5 were expressed in most tissues, with highest levels in liver and kidney, whereas StarD6 was expressed exclusively in the testis. In contrast to StarD4, expression of StarD5 and MLN64 was not sterol-regulated. StarD4, StarD5, and StarD6 may be involved in the intracellular transport of sterols or other lipids.

show abstract

Section: Discussionmentioning

confidence: 99%

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

Soccio

Adams

Romanowski

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

174

162

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“…Intracellular cholesterol is preferentially associated to recycling endosomes (Hao et al, 2002(Hao et al, , 2004, and it has been proposed that this pool of cholesterol favors intracellular retention of raft-associated proteins (Mayor et al, 1998). Therefore, it is tempting to speculate that a localized depletion of cholesterol will favor the mobilization of internalized proteins.…”

Section: Cholesterol Addition Impairs Ltpmentioning

confidence: 99%

LTP-triggered cholesterol redistribution activates Cdc42 and drives AMPA receptor synaptic delivery

Brachet¹,

Norwood²,

Brouwers³

et al. 2015

J Gen Physiol

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“…To reduce artifacts that could coalesce PIP 2 microdomains (50), minimal fixation and no permeabilization were used. Under these conditions, all of the cells were fixed, and most cells were permeabilized (20) to allow staining of actin with phalloidin in PH PLC␦ -GFP-expressing cells. Furthermore, imaging with PH PLC␦ -GFP was shown to yield closely comparable labeling patterns before and after fixation (17).…”

Section: Reduced Membrane Microdomains Enhance Gsis-choles-mentioning

confidence: 99%

“…6, A-C, PH PLC␦ -GFP-expressing cells were fixed with 1% paraformaldehyde for 2 min at 37°C, followed by 15 min in Alexa 546-phalloidin at room temperature. Under this condition, all cells were fixed, and most cells were permeabilized (20) to allow actin staining.…”

mentioning

confidence: 99%

Cholesterol Regulates Glucose-stimulated Insulin Secretion through Phosphatidylinositol 4,5-Bisphosphate

Hao

Bogan

2009

Journal of Biological Chemistry

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Membrane cholesterol modulates the ability of glucose to stimulate insulin secretion from pancreatic ␤-cells. The molecular mechanism by which this occurs is not understood. Here, we show that in cultured ␤-cells, cholesterol acts through phosphatidylinositol 4,5-bisphosphate (PIP 2 ) to regulate actin dynamics, plasma membrane potential, and glucose-stimulated insulin secretion. Cholesterol-overloaded ␤-cells exhibited decreased PIP 2 hydrolysis, with diminished glucose-induced actin reorganization, membrane depolarization, and insulin secretion. The converse findings were observed in cholesteroldepleted cells. These results support a model in which cholesterol depletion is coupled through PIP 2 to enhance both plasma membrane Ca 2؉ influx from the extracellular space, as well as inositol 1,4,5-triphosphate-stimulated Ca 2؉ efflux from intracellular stores. The inability to increase cytosolic Ca 2؉ may be the main underlying factor to account for impaired glucosestimulated insulin secretion in cholesterol-overloaded ␤-cells.

show abstract

Vesicular and Non-vesicular Sterol Transport in Living Cells

Cited by 276 publications

References 77 publications

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

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

LTP-triggered cholesterol redistribution activates Cdc42 and drives AMPA receptor synaptic delivery

Cholesterol Regulates Glucose-stimulated Insulin Secretion through Phosphatidylinositol 4,5-Bisphosphate

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