Proteomics

Dataset Information

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SIRT6 and SIRT7 binding proteome


ABSTRACT: To find the SIRT6 and SIRT7 binding proteins, we expressed V5-tagged SIRT6 and SIRT7 and pulled down this protein with anti-V5 agarose affinity gel. Sirtuins are a family of NAD-dependent deacetylases which deacetylate not only histones but also a wide range of target proteins. Sirtuins are conserved from yeast to mammal, and are known to regulate many processes such as cellular metabolism, apoptosis, cellular senescence, cell cycle, and organism-level aging. Among the members of sirtuins showing different subcellular localization, SIRT1, SIRT6 and SIRT7 are localized in nucleus. Whereas many functions and interacting proteins of SIRT1 have been studied, functions of SIRT6 and SIRT7 are not extensively revealed yet. Since it is important to understand the molecular function of SIRT6 and SIRT7, we here aimed to identify interacting proteins in mammalian cells.
Extra primary submitter: Namgyu Lee, Department of Life Sciences, Pohang University of Science and Technology, Pohang, 790-784, Republic of Korea
Lab head: Kwan Yong Choi, Department of Life Sciences and Division of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang, 790-784, Republ ic of Korea

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Dae-Kyum Kim  

LAB HEAD: Dae-Kyum Kim

PROVIDER: PXD000159 | Pride | 2014-04-28

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
SIRT6.zip Other
SIRT6_negative.raw Raw
SIRT6_negative_120125152541.raw Raw
SIRT6_negative_120125175013.raw Raw
SIRT6_positive.raw Raw
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Publications

Comparative interactomes of SIRT6 and SIRT7: Implication of functional links to aging.

Lee Namgyu N   Kim Dae-Kyum DK   Kim Eung-Sam ES   Park Sung Jin SJ   Kwon Jung-Hee JH   Shin Jihye J   Park Seon-Min SM   Moon Young Ho YH   Wang Hee Jung HJ   Gho Yong Song YS   Choi Kwan Yong KY  

Proteomics 20140528 13-14


Sirtuins are NAD(+) -dependent deacetylases that regulate a range of cellular processes. Although diverse functions of sirtuins have been proposed, those functions of SIRT6 and SIRT7 that are mediated by their interacting proteins remain elusive. In the present study, we identified SIRT6- and SIRT7-interacting proteins, and compared their interactomes to investigate functional links. Our interactomes revealed 136 interacting proteins for SIRT6 and 233 for SIRT7 while confirming seven and 111 pro  ...[more]

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