(Q34456503)

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Identification of functional domains of Mid1, a stretch-activated channel component, necessary for localization to the plasma membrane and Ca2+ permeation

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PubMed publication ID

2 August 2017

Identification of functional domains of Mid1, a stretch-activated channel component, necessary for localization to the plasma membrane and Ca2+ permeation (English)

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Europe PubMed Central

PubMed publication ID

2 August 2017

author name string

Chikako Ozeki-Miyawaki

1

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2 August 2017

Yoshie Moriya

2

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2 August 2017

Hitoshi Tatsumi

3

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2 August 2017

Hidetoshi Iida

4

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2 August 2017

Masahiro Sokabe

5

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2 August 2017

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publication date

3 October 2005

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2 August 2017

Experimental Cell Research

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2 August 2017

311

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2 August 2017

1

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2 August 2017

84-95

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Europe PubMed Central

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2 August 2017

Mechanosensitive channels in prokaryotes.

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MID1, a novel Saccharomyces cerevisiae gene encoding a plasma membrane protein, is required for Ca2+ influx and mating

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yam8(+), a Schizosaccharomyces pombe gene, is a potential homologue of the Saccharomyces cerevisiae MID1 gene encoding a stretch-activated Ca(2+)-permeable channel

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Exiting the endoplasmic reticulum

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The I-II loop of the Ca2+ channel alpha1 subunit contains an endoplasmic reticulum retention signal antagonized by the beta subunit.

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Plasma membrane localization is required for RGS4 function in Saccharomyces cerevisiae

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Molecular dissection of the hydrophobic segments H3 and H4 of the yeast Ca2+ channel component Mid1.

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Evidence for the intimate relationship between vesicle budding from the ER and the unfolded protein response

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New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites

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Involvement of stretch-activated ion channels in Ca2+ mobilization to mechanical stretch in endothelial cells

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Protamine augments stretch induced calcium increase in vascular endothelium

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Direct evidence for ligand-induced internalization of the yeast alpha-factor pheromone receptor

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Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases

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Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins.

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Essential hydrophilic carboxyl-terminal regions including cysteine residues of the yeast stretch-activated calcium-permeable channel Mid1.

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Subcellular localization and oligomeric structure of the yeast putative stretch-activated Ca2+ channel component Mid1.

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Signal peptides: exquisitely designed transport promoters

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Functional compartments of the yeast Golgi apparatus are defined by the sec7 mutation.

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Targeting vesicles to specific sites on the plasma membrane: the role of the sec6/8 complex

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Identifiers

10.1016/J.YEXCR.2005.08.014

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

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