Structure of a 14-3-3 sigma-YAP phosphopeptide complex at 1.15 a resolution

B. Schumacher, M. Skwarczynska, R. Rose, C. Ottmann

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Abstract

The 14-3-3 proteins are a class of eukaryotic acidic adapter proteins, with seven isoforms in humans. 14-3-3 proteins mediate their biological function by binding to target proteins and influencing their activity. They are involved in pivotal pathways in the cell such as signal transduction, gene expression, enzyme activation, cell division and apoptosis. The Yes-associated protein (YAP) is a WW-domain protein that exists in two transcript variants of 48 and 54 kDa in humans. By transducing signals from the cytoplasm to the nucleus, YAP is important for transcriptional regulation. In both variants, interaction with 14-3-3 proteins after phosphorylation of Ser127 is important for nucleocytoplasmic trafficking, via which the localization of YAP is controlled. In this study, 14-3-3 Sigma has been cloned, purified and crystallized in complex with a phosphopeptide from the YAP 14-3-3-binding domain, which led to a crystal that diffracted to 1.15 A resolution. The crystals belonged to space group C222(1), with unit-cell parameters a = 82.3, b = 112.1, c = 62.9 A.
Original languageEnglish
Pages (from-to)978-984
Number of pages7
JournalActa crystallographica. Section F, Structural biology and crystallization communications
Volume66
Issue number9
DOIs
Publication statusPublished - 2010

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Phosphopeptides
14-3-3 Proteins
proteins
Proteins
Enzyme Activation
Signal transduction
Crystals
Phosphorylation
Cell Division
Signal Transduction
Protein Isoforms
Cytoplasm
Gene expression
Apoptosis
adapters
cell division
Gene Expression
Chemical activation
phosphorylation
Cells

Cite this

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title = "Structure of a 14-3-3 sigma-YAP phosphopeptide complex at 1.15 a resolution",
abstract = "The 14-3-3 proteins are a class of eukaryotic acidic adapter proteins, with seven isoforms in humans. 14-3-3 proteins mediate their biological function by binding to target proteins and influencing their activity. They are involved in pivotal pathways in the cell such as signal transduction, gene expression, enzyme activation, cell division and apoptosis. The Yes-associated protein (YAP) is a WW-domain protein that exists in two transcript variants of 48 and 54 kDa in humans. By transducing signals from the cytoplasm to the nucleus, YAP is important for transcriptional regulation. In both variants, interaction with 14-3-3 proteins after phosphorylation of Ser127 is important for nucleocytoplasmic trafficking, via which the localization of YAP is controlled. In this study, 14-3-3 Sigma has been cloned, purified and crystallized in complex with a phosphopeptide from the YAP 14-3-3-binding domain, which led to a crystal that diffracted to 1.15 A resolution. The crystals belonged to space group C222(1), with unit-cell parameters a = 82.3, b = 112.1, c = 62.9 A.",
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Structure of a 14-3-3 sigma-YAP phosphopeptide complex at 1.15 a resolution. / Schumacher, B.; Skwarczynska, M.; Rose, R.; Ottmann, C.

In: Acta crystallographica. Section F, Structural biology and crystallization communications, Vol. 66, No. 9, 2010, p. 978-984.

Research output: Contribution to journalArticleAcademicpeer-review

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AB - The 14-3-3 proteins are a class of eukaryotic acidic adapter proteins, with seven isoforms in humans. 14-3-3 proteins mediate their biological function by binding to target proteins and influencing their activity. They are involved in pivotal pathways in the cell such as signal transduction, gene expression, enzyme activation, cell division and apoptosis. The Yes-associated protein (YAP) is a WW-domain protein that exists in two transcript variants of 48 and 54 kDa in humans. By transducing signals from the cytoplasm to the nucleus, YAP is important for transcriptional regulation. In both variants, interaction with 14-3-3 proteins after phosphorylation of Ser127 is important for nucleocytoplasmic trafficking, via which the localization of YAP is controlled. In this study, 14-3-3 Sigma has been cloned, purified and crystallized in complex with a phosphopeptide from the YAP 14-3-3-binding domain, which led to a crystal that diffracted to 1.15 A resolution. The crystals belonged to space group C222(1), with unit-cell parameters a = 82.3, b = 112.1, c = 62.9 A.

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