Inositol 1,4,5‐trisphosphate releases Ca<sup>2+</sup> from vacuolar membrane vesicles of <i>Saccharomyces cerevisiae</i>

Belde, P.J.M.; Vossen, Jack H.; Borst-Pauwels, G.W.F.H.; Theuvenet, A.P.R.

doi:10.1016/0014-5793(93)81460-h

Cited by 69 publications

(48 citation statements)

References 40 publications

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“…The difference in inhibitor signatures indicates that the large conductance channel is localized in vacuoles as TMB-8, dantrolene and heparin are widely reported to inhibit the IP3-induced Ca 2+ release from vacuoles in S. cerevisiae [TMB-8 and dantrolene (Belde et al, 1993)], in N. crassa [dantrolene (Cornelius et al, 1989)], in red beet root [heparin and TMB-8 (Brosnan and Sanders, 1990;Alexandre et al, 1990)], and C. albicans [partial inhibition by heparin (Calvert and Sanders, 1995)]. The localization of the large conductance channel on step gradients confirms its origin as vacuolar.…”

Section: Discussionmentioning

confidence: 99%

An IP3-activated Ca2+ channel regulates fungal tip growth

Silverman‐Gavrila

Lew

2002

Journal of Cell Science

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Hyphal extension in fungi requires a tip-high Ca2+ gradient,which is generated and maintained internally by inositol (1,4,5)-trisphosphate(IP3)-induced Ca2+ release from tip-localized vesicles and subapical Ca2+ sequestration. Using the planar bilayer method we demonstrated the presence of two types of IP3-activated Ca2+ channels in Neurospora crassa membranes with different conductances: one low (13 picosiemens), the other high (77 picosiemens). On sucrose density gradients the low conductance channel co-localized with endoplasmic reticulum and plasma membrane, and the high conductance channel co-localized with vacuolar membranes. We correlated the effect of inhibitors on channel activity with their effect on hyphal growth and Ca2+ gradients. The inhibitor of IP3-induced Ca2+ release, 2-aminoethoxidiphenylborate (2-APB), inhibits both channels, while heparin, 8-(N,N-diethylamino)-octyl-3,4,5-trimethoxybenzoate,hydrochloride (TMB-8) and dantrolene inhibit only the large conductance channel. Because 2-APB inhibits hyphal growth and dissipates the tip-high cytosolic [Ca2+] gradient, whereas heparin microinjection, TMB-8 and dantrolene treatments do not affect growth, we suggest that the small conductance channel generates the obligatory tip-high Ca2+ gradient during hyphal growth. Since IP3 production must be catalyzed by tip-localized phospholipase C, we show that a number of phospholipase C inhibitors [neomycin,1-[6-((17β-3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl]-1H-pyrrole-2,5-dione (U-73122) (but not the inactive pyrrolidine U-73343),3-nitrocoumarin] inhibit hyphal growth and affect, similarly to 2-APB, the location of vesicular Ca2+ imaged by chlortetracycline staining.

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Section: Discussionmentioning

confidence: 99%

An IP3-activated Ca2+ channel regulates fungal tip growth

Silverman‐Gavrila

Lew

2002

Journal of Cell Science

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“…It has previously been demonstrated that Ca 2ϩ mobilization through IP 3 receptors is required for nuclear fusion (41), in vitro liposome fusion (11), and the fusion of secretory granules with the plasma membrane (18). Moreover, Ca 2ϩ is stored in the vacuole and IP 3 has previously been shown to stimulate its release (4). Third, the products of phospholipase D and phospholipase C may create a membrane section that is physically capable of undergoing membrane fusion by changing the phospholipid composition (18,38).…”

Section: Discussionmentioning

confidence: 99%

Vac7p, a Novel Vacuolar Protein, Is Required for Normal Vacuole Inheritance and Morphology

Bonangelino

Catlett

Weisman

1997

Molecular and Cellular Biology

118

150

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During cell division, the vacuole of Saccharomyces cerevisiae partitions between mother and daughter cells. A portion of the parental vacuole membrane moves into the bud, and ultimately membrane scission divides the vacuole into two separate structures. Here we characterize two yeast mutations causing defects in vacuole membrane scission, vac7-1 and vac14-1. A third mutant, a fab1-2 strain, isolated in a nonrelated screen (A. Yamamoto et al., Mol. Biol. Cell 6:525-539, 1995) shares the vacuolar phenotypes of the vac7-1 and vac14-1 strains. Unlike the wild type, mutant vacuoles are not multilobed structures; in many cases, a single vacuole spans both the mother and bud, with a distinct gap in the mother-bud neck. Thus, even where the membranes are closely opposed, vacuole fission is arrested. Simply enlarging the vacuole does not produce this mutant phenotype. An additional common phenotype of these mutants is a defect in vacuole acidification; however, vacuole scission in most other vacuole acidification mutants is normal. An alteration in vacuole membrane lipids could account for both the vacuole membrane scission and acidification defects. Because a directed screen has not identified additional class III complementation groups, it is likely that all three genes are involved in a similar process. Interestingly, FAB1, was previously shown to encode a putative phosphatidylinositol-4-phosphate 5-kinase. Moreover, overexpression of FAB1 suppresses the vac14-1 mutation, which suggests that VAC14 and FAB1 act at a common step. VAC7 encodes a novel 128-kDa protein that is localized at the vacuole membrane. This location of Vac7p is consistent with its involvement in vacuole morphology and inheritance.

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“…It has been shown that inositol trisphosphate (IP 3 ) releases vacuolar Ca 2ϩ through an as yet unknown channel (26). Additionally, mTRP3 is activated by IP 3 by direct interaction with the IP 3 receptor (27).…”

Section: Resultsmentioning

confidence: 99%

A TRP homolog in Saccharomyces cerevisiae forms an intracellular Ca ²⁺ -permeable channel in the yeast vacuolar membrane

Palmer

Zhou

Lin

et al. 2001

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

216

224

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The molecular identification of ion channels in internal membranes has made scant progress compared with the study of plasma membrane ion channels. We investigated a prominent voltagedependent, cation-selective, and calcium-activated vacuolar ion conductance of 320 pS (yeast vacuolar conductance, YVC1) in Saccharomyces cerevisiae. Here we report on a gene, the deduced product of which possesses significant homology to the ion channel of the transient receptor potential (

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Inositol 1,4,5‐trisphosphate releases Ca²⁺ from vacuolar membrane vesicles of Saccharomyces cerevisiae

Cited by 69 publications

References 40 publications

An IP3-activated Ca2+ channel regulates fungal tip growth

An IP3-activated Ca2+ channel regulates fungal tip growth

Vac7p, a Novel Vacuolar Protein, Is Required for Normal Vacuole Inheritance and Morphology

A TRP homolog in Saccharomyces cerevisiae forms an intracellular Ca ²⁺ -permeable channel in the yeast vacuolar membrane

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Inositol 1,4,5‐trisphosphate releases Ca2+ from vacuolar membrane vesicles of Saccharomyces cerevisiae

Cited by 69 publications

References 40 publications

An IP3-activated Ca2+ channel regulates fungal tip growth

An IP3-activated Ca2+ channel regulates fungal tip growth

Vac7p, a Novel Vacuolar Protein, Is Required for Normal Vacuole Inheritance and Morphology

A TRP homolog in Saccharomyces cerevisiae forms an intracellular Ca 2+ -permeable channel in the yeast vacuolar membrane

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Inositol 1,4,5‐trisphosphate releases Ca²⁺ from vacuolar membrane vesicles of Saccharomyces cerevisiae

A TRP homolog in Saccharomyces cerevisiae forms an intracellular Ca ²⁺ -permeable channel in the yeast vacuolar membrane