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Hiroko Hama

Researcher at Utah State University

Publications -  11
Citations -  1291

Hiroko Hama is an academic researcher from Utah State University. The author has contributed to research in topics: Golgi apparatus & Phosphatidylinositol. The author has an hindex of 11, co-authored 11 publications receiving 1263 citations. Previous affiliations of Hiroko Hama include University of Texas Southwestern Medical Center.

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Direct involvement of phosphatidylinositol 4-phosphate in secretion in the yeast Saccharomyces cerevisiae.

TL;DR: Findings indicate that, first, PtdIns(4)P limitation is a major contributing factor to the secretory defect in sec14 cells; second, Sec14p function is coupled to the action of Pik1p, and; third, PTDIns( 4)P has an important role in the Golgi-to-plasma membrane stage of secretion.
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Rapid Accumulation of Phosphatidylinositol 4,5-Bisphosphate and Inositol 1,4,5-Trisphosphate Correlates with Calcium Mobilization in Salt-Stressed Arabidopsis

TL;DR: It is reported that Arabidopsis plants grown in liquid media rapidly increase PtdIns(4,5)P(2) synthesis in response to treatment with sodium chloride, potassium chloride, and sorbitol, and this data suggest that when challenged with salinity and osmotic stress, terrestrial plants respond differently than algae, yeasts, and animal cells that accumulate different species of phosphoinositides.
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The Phosphatidylinositol 3-Phosphate Binding Protein Vac1p Interacts with a Rab GTPase and a Sec1p Homologue to Facilitate Vesicle-mediated Vacuolar Protein Sorting

TL;DR: It is proposed that activated-Vps21p interacts with its effector, Vac1p, which interacts with Vps45p to regulate the Golgi to endosome SNARE complex.
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Vps9p Is a Guanine Nucleotide Exchange Factor Involved in Vesicle-mediated Vacuolar Protein Transport

TL;DR: It is concluded that Vps9p is a novel guanine nucleotide exchange factor that is specific for Vps21p/Rab5 and may also possess unique regulatory functions required for vacuolar protein transport.
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Yeast phosphatidylinositol 4-kinase, Pik1, has essential roles at the Golgi and in the nucleus.

TL;DR: Catalytically inactive derivatives of these compartment-restricted Pik1 constructs indicated that PtdIns4P must be generated both in the nucleus and at the Golgi for normal cell function.