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Papers by Eriko Michishita-kioi

Research paper thumbnail of SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation. Nature. 2012; 487: p

Research paper thumbnail of Finding a target for resveratrol

Research paper thumbnail of SIRT7 inactivation reverses metastatic phenotypes in epithelial and mesenchymal tumors

Scientific reports, Jan 29, 2015

Metastasis is responsible for over 90% of cancer-associated mortality. In epithelial carcinomas, ... more Metastasis is responsible for over 90% of cancer-associated mortality. In epithelial carcinomas, a key process in metastatic progression is the epigenetic reprogramming of an epithelial-to-mesenchymal transition-like (EMT) change towards invasive cellular phenotypes. In non-epithelial cancers, different mechanisms must underlie metastatic change, but relatively little is known about the factors involved. Here, we identify the chromatin regulatory Sirtuin factor SIRT7 as a key regulator of metastatic phenotypes in both epithelial and mesenchymal cancer cells. In epithelial prostate carcinomas, high SIRT7 levels are associated with aggressive cancer phenotypes, metastatic disease, and poor patient prognosis, and depletion of SIRT7 can reprogram these cells to a less aggressive phenotype. Interestingly, SIRT7 is also important for maintaining the invasiveness and metastatic potential of non-epithelial sarcoma cells. Moreover, SIRT7 inactivation dramatically suppresses cancer cell metas...

Research paper thumbnail of Proteomic analysis of the SIRT6 interactome: novel links to genome maintenance and cellular stress signaling

Scientific Reports, 2013

The chromatin regulatory factor SIRT6 plays pivotal roles in metabolism, tumor suppression, and a... more The chromatin regulatory factor SIRT6 plays pivotal roles in metabolism, tumor suppression, and aging biology. Despite the fundamental roles of SIRT6 in physiology and disease, only a handful of molecular and functional interactions of SIRT6 have been reported. Here, we characterize the SIRT6 interactome and identify 801 novel SIRT6-interacting proteins. The discovery of these SIRT6-associations considerably expands knowledge of the SIRT6 interaction network, and suggests previously unknown functional interactions of SIRT6 in fundamental cellular processes. These include chromatin remodeling, mitotic chromosome segregation, protein homeostasis, and transcriptional elongation. Extended analysis of the SIRT6 interaction with G3BP1, a master stress response factor, uncovers an unexpected role and mechanism of SIRT6 in regulating stress granule assembly and cellular stress resistance.

Research paper thumbnail of SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation

Nature, 2012

Sirtuin proteins regulate diverse cellular pathways that influence genomic stability, metabolism ... more Sirtuin proteins regulate diverse cellular pathways that influence genomic stability, metabolism and ageing. SIRT7 is a mammalian sirtuin whose biochemical activity, molecular targets and physiological functions have been unclear. Here we show that SIRT7 is an NAD+-dependent ...

Research paper thumbnail of SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation. Nature. 2012; 487: p

Research paper thumbnail of Finding a target for resveratrol

Research paper thumbnail of SIRT7 inactivation reverses metastatic phenotypes in epithelial and mesenchymal tumors

Scientific reports, Jan 29, 2015

Metastasis is responsible for over 90% of cancer-associated mortality. In epithelial carcinomas, ... more Metastasis is responsible for over 90% of cancer-associated mortality. In epithelial carcinomas, a key process in metastatic progression is the epigenetic reprogramming of an epithelial-to-mesenchymal transition-like (EMT) change towards invasive cellular phenotypes. In non-epithelial cancers, different mechanisms must underlie metastatic change, but relatively little is known about the factors involved. Here, we identify the chromatin regulatory Sirtuin factor SIRT7 as a key regulator of metastatic phenotypes in both epithelial and mesenchymal cancer cells. In epithelial prostate carcinomas, high SIRT7 levels are associated with aggressive cancer phenotypes, metastatic disease, and poor patient prognosis, and depletion of SIRT7 can reprogram these cells to a less aggressive phenotype. Interestingly, SIRT7 is also important for maintaining the invasiveness and metastatic potential of non-epithelial sarcoma cells. Moreover, SIRT7 inactivation dramatically suppresses cancer cell metas...

Research paper thumbnail of Proteomic analysis of the SIRT6 interactome: novel links to genome maintenance and cellular stress signaling

Scientific Reports, 2013

The chromatin regulatory factor SIRT6 plays pivotal roles in metabolism, tumor suppression, and a... more The chromatin regulatory factor SIRT6 plays pivotal roles in metabolism, tumor suppression, and aging biology. Despite the fundamental roles of SIRT6 in physiology and disease, only a handful of molecular and functional interactions of SIRT6 have been reported. Here, we characterize the SIRT6 interactome and identify 801 novel SIRT6-interacting proteins. The discovery of these SIRT6-associations considerably expands knowledge of the SIRT6 interaction network, and suggests previously unknown functional interactions of SIRT6 in fundamental cellular processes. These include chromatin remodeling, mitotic chromosome segregation, protein homeostasis, and transcriptional elongation. Extended analysis of the SIRT6 interaction with G3BP1, a master stress response factor, uncovers an unexpected role and mechanism of SIRT6 in regulating stress granule assembly and cellular stress resistance.

Research paper thumbnail of SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation

Nature, 2012

Sirtuin proteins regulate diverse cellular pathways that influence genomic stability, metabolism ... more Sirtuin proteins regulate diverse cellular pathways that influence genomic stability, metabolism and ageing. SIRT7 is a mammalian sirtuin whose biochemical activity, molecular targets and physiological functions have been unclear. Here we show that SIRT7 is an NAD+-dependent ...

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