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Nature
Resumen/Descripción – provisto por la editorial en inglés
Nature is a weekly international journal publishing the finest peer-reviewed research in all fields of science and technology on the basis of its originality, importance, interdisciplinary interest, timeliness, accessibility, elegance and surprising conclusions. Nature also provides rapid, authoritative, insightful and arresting news and interpretation of topical and coming trends affecting science, scientists and the wider public.Palabras clave – provistas por la editorial
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Disponibilidad
| Institución detectada | Período | Navegá | Descargá | Solicitá |
|---|---|---|---|---|
| No detectada | desde jul. 2012 / hasta dic. 2023 | Nature.com | ||
| No detectada | desde jul. 2006 / hasta ago. 2012 | Ovid |
Información
Tipo de recurso:
revistas
ISSN impreso
0028-0836
ISSN electrónico
1476-4687
Editor responsable
Springer Nature
País de edición
Reino Unido
Fecha de publicación
1869-
Tabla de contenidos
Grace and flavour, under pressure
M. E. Garber
Palabras clave: Multidisciplinary.
Pp. No disponible
How climate change could drive an increase in gender-based violence
Meghie Rodrigues
Palabras clave: Multidisciplinary.
Pp. No disponible
Historic dive aims to map Earth’s deepest point like never before
Freda Kreier
Palabras clave: Multidisciplinary.
Pp. No disponible
More than dollars: mega-review finds 50 ways to value nature
Ehsan Masood
Palabras clave: Multidisciplinary.
Pp. No disponible
UK graduate students demand pay rise from nation’s largest research funder
Chris Woolston
Palabras clave: Multidisciplinary.
Pp. No disponible
Ancient mud reveals the longest record of climate from the tropics
Nick Petrić Howe; Shamini Bundell
Palabras clave: Multidisciplinary.
Pp. No disponible
Structure of the MRAS–SHOC2–PP1C phosphatase complex
Zachary J. Hauseman
; Michelle Fodor; Anxhela Dhembi; Jessica Viscomi; David Egli; Melusine Bleu; Stephanie Katz; Eunyoung Park; Dong Man Jang; Kathryn A. Porter; Fabian Meili; Hongqiu Guo; Grainne Kerr; Sandra Mollé; Camilo Velez-Vega; Kim S. Beyer; Giorgio G. Galli; Saveur-Michel Maira; Travis Stams; Kirk Clark; Michael J. Eck; Luca Tordella; Claudio R. Thoma; Daniel A. King
<jats:title>Abstract</jats:title><jats:p>RAS–MAPK signalling is fundamental for cell proliferation and is altered in most human cancers<jats:sup>1–3</jats:sup>. However, our mechanistic understanding of how RAS signals through RAF is still incomplete. Although studies revealed snapshots for autoinhibited and active RAF–MEK1–14-3-3 complexes<jats:sup>4</jats:sup>, the intermediate steps that lead to RAF activation remain unclear. The MRAS–SHOC2–PP1C holophosphatase dephosphorylates RAF at serine 259, resulting in the partial displacement of 14-3-3 and RAF–RAS association<jats:sup>3,5,6</jats:sup>. MRAS, SHOC2 and PP1C are mutated in rasopathies—developmental syndromes caused by aberrant MAPK pathway activation<jats:sup>6–14</jats:sup>—and SHOC2 itself has emerged as potential target in receptor tyrosine kinase (RTK)–RAS-driven tumours<jats:sup>15–18</jats:sup>. Despite its importance, structural understanding of the SHOC2 holophosphatase is lacking. Here we determine, using X-ray crystallography, the structure of the MRAS–SHOC2–PP1C complex. SHOC2 bridges PP1C and MRAS through its concave surface and enables reciprocal interactions between all three subunits. Biophysical characterization indicates a cooperative assembly driven by the MRAS GTP-bound active state, an observation that is extendible to other RAS isoforms. Our findings support the concept of a RAS-driven and multi-molecular model for RAF activation in which individual RAS–GTP molecules recruit RAF–14-3-3 and SHOC2–PP1C to produce downstream pathway activation. Importantly, we find that rasopathy and cancer mutations reside at protein–protein interfaces within the holophosphatase, resulting in enhanced affinities and function. Collectively, our findings shed light on a fundamental mechanism of RAS biology and on mechanisms of clinically observed enhanced RAS–MAPK signalling, therefore providing the structural basis for therapeutic interventions.</jats:p>
Palabras clave: Multidisciplinary.
Pp. No disponible
Structure–function analysis of the SHOC2–MRAS–PP1C holophosphatase complex
Jason J. Kwon; Behnoush Hajian; Yuemin Bian; Lucy C. Young; Alvaro J. Amor; James R. Fuller; Cara V. Fraley; Abbey M. Sykes; Jonathan So; Joshua Pan; Laura Baker; Sun Joo Lee; Douglas B. Wheeler; David L. Mayhew; Nicole S. Persky; Xiaoping Yang; David E. Root; Anthony M. Barsotti; Andrew W. Stamford; Charles K. Perry; Alex Burgin; Frank McCormick; Christopher T. Lemke; William C. Hahn; Andrew J. Aguirre
Palabras clave: Multidisciplinary.
Pp. No disponible
The knotty problem of tuning an instrument
Palabras clave: Multidisciplinary.
Pp. No disponible
Seven questions to ask before pursuing a new grant
Betty Lai
Palabras clave: Multidisciplinary.
Pp. No disponible