The Sec14-superfamily and the regulatory interface between phospholipid metabolism and membrane trafficking

Mousley, Carl J.; Tyeryar, Kimberly R.; Vincent-Pope, Patrick; Bankaitis, Vytas A.

doi:10.1016/j.bbalip.2007.04.002

Cited by 73 publications

(63 citation statements)

References 66 publications

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“…Similar results were observed for clavesin 2 in neurons and for both clavesin 1 and 2 ectopically expressed in HeLa cells (data not shown). The Sec14 Domain of Clavesin 1 Binds PtdIns(3,5)P 2 -Sec14 domains generally function in lipid binding (21,22). Preliminary studies with PIP strips indicated that the Sec14 domain of clavesin 1 and 2 bound to phosphorylated forms of PtdIns but not PtdIns alone or other phospholipids, such as phosphatidylcholine or phosphatidylserine (data not shown).…”

Section: Resultsmentioning

confidence: 99%

“…Sec14p is composed of the Sec14 domain only, whereas the majority of Sec14 proteins in mammals contain a Sec14 domain in conjunction with other modules or protein/lipid binding domains (21,22). In the few well characterized examples, these proteins function to integrate lipid binding/metabolism with other biological functions (21,22).…”

mentioning

confidence: 99%

“…Yeast Sec14p is a phospholipid transfer protein that extracts phosphatidylinositol and phosphatidylcholine from membranes in vitro and regulates the metabolism of these lipids in cells (19,20). Sec14p is composed of the Sec14 domain only, whereas the majority of Sec14 proteins in mammals contain a Sec14 domain in conjunction with other modules or protein/lipid binding domains (21,22). In the few well characterized examples, these proteins function to integrate lipid binding/metabolism with other biological functions (21,22).…”

mentioning

confidence: 99%

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The Clavesin Family, Neuron-specific Lipid- and Clathrin-binding Sec14 Proteins Regulating Lysosomal Morphology

Katoh

Ritter

Gaffry

et al. 2009

Journal of Biological Chemistry

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Clathrin-coated vesicles (CCVs) originating from the transGolgi network (TGN) provide a major transport pathway from the secretory system to endosomes/lysosomes. Herein we describe paralogous Sec14 domain-bearing proteins, clavesin 1/CRALBPL and clavesin 2, identified through a proteomic analysis of CCVs. Clavesins are enriched on CCVs and form a complex with clathrin heavy chain (CHC) and adaptor protein-1, major coat components of TGN-derived CCVs. The proteins co-localize with markers of endosomes and the TGN as well as with CHC and adaptor protein-1. A membrane mimic assay using the Sec14 domain of clavesin 1 reveals phosphatidylinositol 3,5-bisphosphate as a specific lipid partner. Phosphatidylinositol 3,5-bisphosphate is localized to late endosomes/lysosomes, and interestingly, isoform-specific knockdown of clavesins in neurons using lentiviral delivery of interfering RNA leads to enlargement of a lysosome-associated membrane protein 1-positive membrane compartment with no obvious influence on the CCV machinery at the TGN. Since clavesins are expressed exclusively in neurons, this new protein family appears to provide a unique neuron-specific regulation of late endosome/lysosome morphology.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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The Clavesin Family, Neuron-specific Lipid- and Clathrin-binding Sec14 Proteins Regulating Lysosomal Morphology

Katoh

Ritter

Gaffry

et al. 2009

Journal of Biological Chemistry

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“…The association of transiently increased neural PtdCho (in OP-dosed mice) with degeneration confined to the longest spinal axons and of sustained PtdCho elevation (in NTE-cKO mice) with increasing areas of axonal damage suggests a linkage between neural PtdCho homeostasis and axonal maintenance. In yeast, PtdCho homeostasis and constitutive secretion are linked via the phospholipid-binding protein, sec14p (Mousley et al, 2007). Axonal maintenance depends on membrane trafficking and microtubule-based transport.…”

Section: Discussionmentioning

confidence: 99%

Neuropathy Target Esterase Is Required for Adult Vertebrate Axon Maintenance

Read¹,

Li²,

Chao³

et al. 2009

J. Neurosci.

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The enzyme neuropathy target esterase (NTE) is present in neurons and deacylates the major membrane phospholipid, phosphatidylcholine (PtdCho). Mutation of the NTE gene or poisoning by neuropathic organophosphates-chemical inhibitors of NTE-causes distal degeneration of long spinal axons in humans. However, analogous neuropathological changes have not been reported in nestincre:NTEfl/fl mice with NTE-deficient neural tissue. Furthermore, altered PtdCho homeostasis has not been detected in NTE-deficient vertebrates. Here, we describe distal degeneration of the longest spinal axons in ϳ3-week-old nestin-cre:NTEfl/fl mice and in adult C57BL/6J mice after acute dosing with a neuropathic organophosphate: in both groups early degenerative lesions were followed by swellings comprising accumulated axoplasmic material. In mice dosed acutely with organophosphate, maximal numbers of lesions, in the longest spinal sensory axon tract, were attained within days and were preceded by a transient rise in neural PtdCho. In nestin-cre: NTEfl/fl mice, sustained elevation of PtdCho over many months was accompanied by progressive degeneration and massive swelling of axons in sensory and motor spinal tracts and by increasing hindlimb dysfunction. Axonal lesion distribution closely resembled that in hereditary spastic paraplegia (HSP). The importance of defective membrane trafficking in HSP and the association of NTE with the endoplasmic reticulum-the starting point for the constitutive secretory pathway and transport of neuronal materials into axonsprompted investigation for a role of NTE in secretion. Cultured NTE-deficient neurons displayed modestly impaired secretion, consistent with neuronal viability and damage in vivo initially restricted to distal parts of the longest axons.

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“…Therefore, oxysterol-binding proteins might function as sensors rather than transporters (Raychaudhuri and Prinz, 2010). A role as sensors in regulating vesicular transport has been proposed for PI-transfer proteins in yeast (Mousley et al, 2007).…”

Section: Lipid Transportmentioning

confidence: 99%