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A new phosphate-starvation response in fission yeast requires the endocytic function of myosin I

ABSTRACT: This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

ORGANISM(S): Schizosaccharomyces pombe

SUBMITTER: Felix Krueger

PROVIDER: E-GEOD-67126 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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A new phosphate-starvation response in fission yeast requires the endocytic function of myosin I.

Petrini Edoardo E Baillet Victoire V Cridge Jake J Hogan Cassandra J CJ Guillaume Cindy C Ke Huiling H Brandetti Elisa E Walker Simon S Koohy Hashem H Spivakov Mikhail M Varga-Weisz Patrick P

Journal of cell science 20150907 20

Endocytosis is essential for uptake of many substances into the cell, but how it links to nutritional signalling is poorly understood. Here, we show a new role for endocytosis in regulating the response to low phosphate in Schizosaccharomyces pombe. Loss of function of myosin I (Myo1), Sla2/End4 or Arp2, proteins involved in the early steps of endocytosis, led to increased proliferation in low-phosphate medium compared to controls. We show that once cells are deprived of phosphate they undergo a ...[more]

PMID: 26345368

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A novel phosphate-starvation response in fission yeast requires the endocytic function of Myosin I (RNA-seq)

Project description:S. pombe Myosin I (MyoI) plays a key role in cytoskeletal functions, in particular it is part of the endocytotic machinery. Here we show a novel role for MyoI in regulating the response to low phosphate stress. Deletion of MyoI led to an increased proliferation in low phosphate media when compared to a control strain; mutations in other proteins involved in the early steps of endocytosis, such as ARP2 and Sla2/END4, led to the same phenotype. We show that once cells are deprived of phosphate they undergo clear morphological changes, slow down growth but retain viability. This is reminiscent of a quiescence response, and it is completely abolished when MyoI is absent. Transcriptomic analysis revealed a wide perturbation of gene expression upon phosphate starvation, with rapid induction of stress-regulated genes. However, Æmyo1 cells displayed little or negligible effects at gene expression level when they were phosphate-starved. Using a combination of super resolution microscopy and genetic approaches we pinpointed the specific function of MyoI in endocytosis as critical for the response to low phosphate stress. Furthermore, introduction of point-mutated MyoI (with ablated endocytic function) into a ÆmyoI background failed to restore phosphate stress response. Taken together, our data indicate how endocytosis, and in particular MyoI, play a pivotal role in mediating cellular response to nutrients, bridging the external environment and internal molecular functions of the cells. RNA-seq transcriptomic analysis in control and ∆myo1 S.pombe strains comparing gene expression profiles at 4 and 10 hours after phosphate depletion.

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A novel phosphate-starvation response in fission yeast requires the endocytic function of Myosin I (ChIP-seq)

Project description:S. pombe Myosin I (MyoI) plays a key role in cytoskeletal functions, in particular it is part of the endocytotic machinery. Here we show a novel role for MyoI in regulating the response to low phosphate stress. Deletion of MyoI led to an increased proliferation in low phosphate media when compared to a control strain; mutations in other proteins involved in the early steps of endocytosis, such as ARP2 and Sla2/END4, led to the same phenotype. We show that once cells are deprived of phosphate they undergo clear morphological changes, slow down growth but retain viability. This is reminiscent of a quiescence response, and it is completely abolished when MyoI is absent. Transcriptomic analysis revealed a wide perturbation of gene expression upon phosphate starvation, with rapid induction of stress-regulated genes. However, Æmyo1 cells displayed little or negligible effects at gene expression level when they were phosphate-starved. Using a combination of super resolution microscopy and genetic approaches we pinpointed the specific function of MyoI in endocytosis as critical for the response to low phosphate stress. Furthermore, introduction of point-mutated MyoI (with ablated endocytic function) into a ÆmyoI background failed to restore phosphate stress response. Taken together, our data indicate how endocytosis, and in particular MyoI, play a pivotal role in mediating cellular response to nutrients, bridging the external environment and internal molecular functions of the cells. ChIP-seq analysis of Myo1-GFP genomic binding in control or low phosphate condition

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