COPII-Coated Vesicle Formation Reconstituted with Purified Coat Proteins and Chemically Defined Liposomes

Matsuoka, Ken; Orci, Lelio; Amherdt, M; Bednarek, Sebastian Y.; Hamamoto, Susan; Schekman, Randy; Yeung, Thomas

doi:10.1016/s0092-8674(00)81577-9

Cited by 587 publications

(622 citation statements)

References 48 publications

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“…This is surprising, given the fact that in vitro budding of vesicles from chemically defined liposomes is sensitive to the degree of lipid desaturation (Matsuoka et al, 1998). This observation suggests that vesicle formation in vivo might be less sensitive to the acyl chain composition of the lipids or that the lipid pool of the secretory pathway is not immediately affected by a lack of desaturase function.…”

Section: Discussionmentioning

confidence: 99%

Lipid-dependent Subcellular Relocalization of the Acyl Chain Desaturase in Yeast

Tatzer¹,

Zellnig

Kohlwein

et al. 2002

MBoC

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The degree of acyl chain desaturation of membrane lipids is a critical determinant of membrane fluidity. Temperature-sensitive mutants of the single essential acyl chain desaturase, Ole1p, of yeast have previously been isolated in screens for mitochondrial inheritance mutants (Stewart, L.C., and Yaffe, M.P. ). J. Cell Biol. 115, 1249 -1257. We now report that the mutant desaturase relocalizes from its uniform ER distribution to a more punctuate localization at the cell periphery upon inactivation of the enzyme. This relocalization takes place within minutes at nonpermissive conditions, a time scale at which mitochondrial morphology and inheritance is not yet affected. Relocalization of the desaturase is fully reversible and does not affect the steady state localization of other ER resident proteins or the kinetic and fidelity of the secretory pathway, indicating a high degree of selectivity for the desaturase. Relocalization of the desaturase is energy independent but is lipid dependent because it is rescued by supplementation with unsaturated fatty acids. Relocalization of the desaturase is also observed in cells treated with inhibitors of the enzyme, indicating that it is independent of temperature-induced alterations of the enzyme. In the absence of desaturase function, lipid synthesis continues, resulting in the generation of lipids with saturated acyl chains. A model is discussed in which the accumulation of saturated lipids in a microdomain around the desaturase could induce the observed segregation and relocalization of the enzyme.

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Section: Discussionmentioning

confidence: 99%

Lipid-dependent Subcellular Relocalization of the Acyl Chain Desaturase in Yeast

Tatzer¹,

Zellnig

Kohlwein

et al. 2002

MBoC

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“…The ER and nuclear membrane contain ϳ10% of the cellular PtdIns(4,5)P 2 labeled with a PH domain probe (375). The COPII coat responsible for membrane protein export from the ER preferentially binds to acidic phospholipids but does not show a preference for specific PIPs (221). Several PI kinases and phosphatases are located on the ER, but the exact role that they play in secretion, if any, is not known (224,389,392).…”

Section: F Phosphoinositides On the Ermentioning

confidence: 99%

Phosphoinositides in Constitutive Membrane Traffic

Roth

2004

Physiological Reviews

265

267

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Proteins that make, consume, and bind to phosphoinositides are important for constitutive membrane traffic. Different phosphoinositides are concentrated in different parts of the central vacuolar pathway, with phosphatidylinositol 4-phosphate predominate on Golgi, phosphatidylinositol 4,5-bisphosphate predominate at the plasma membrane, phosphatidylinositol 3-phosphate the major phosphoinositide on early endosomes, and phosphatidylinositol 3,5-bisphosphate found on late endocytic organelles. This spatial segregation may be the mechanism by which the direction of membrane traffic is controlled. Phosphoinositides increase the affinity of membranes for peripheral membrane proteins that function for sorting protein cargo or for the docking and fusion of transport vesicles. This implies that constitutive membrane traffic may be regulated by the mechanisms that control the activity of the enzymes that produce and consume phosphoinositides. Although the lipid kinases and phosphatases that function in constitutive membrane traffic are beginning to be identified, their regulation is poorly understood.

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“…Where there is some question about the tendency of a protein to precipitate, an approach in which vesicles are 'floated' in a sucrose gradient may be more appropriate (e.g. [44]), if a little more cumbersome to quantitate. Precipitated protein will pellet in a sucrose gradient, while vesicle-bound protein will migrate (float) with the less-dense vesicles and can thus be readily distinguished (provided that the extent of protein binding does not significantly increase vesicle density).…”

Section: 32mentioning

confidence: 99%

Determining selectivity of phosphoinositide-binding domains

Narayan

Lemmon

2006

Methods

119

121

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The burgeoning of phosphoinositide-binding domains and proteins in cellular signaling and trafficking has drawn laboratories from a wide variety of fields into the study of lipid interactions with peripheral membrane proteins. Many different approaches have been developed to assess phosphoinositide binding, some of which are more problematic than others, and some of which can be quantitated more readily than others. With a focus on the methods used in our laboratory, we describe here the considerations that need to be taken into account when establishing -and quantitating -the specific binding of a protein or domain to phosphoinositides in membranes. We also discuss briefly a few examples in which no clear consensus has yet been reached as to the specificity of a given domain or protein because of discrepancies between different commonlyused approaches.

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COPII-Coated Vesicle Formation Reconstituted with Purified Coat Proteins and Chemically Defined Liposomes

Cited by 587 publications

References 48 publications

Lipid-dependent Subcellular Relocalization of the Acyl Chain Desaturase in Yeast

Lipid-dependent Subcellular Relocalization of the Acyl Chain Desaturase in Yeast

Phosphoinositides in Constitutive Membrane Traffic

Determining selectivity of phosphoinositide-binding domains

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