Non-cooperative 4E-BP2 folding with exchange between eIF4E-binding and binding-incompatible states tunes cap-dependent translation inhibition

Autor: Jennifer E. Dawson, Alaji Bah, Zhenfu Zhang, Robert M. Vernon, Hong Lin, P. Andrew Chong, Manasvi Vanama, Nahum Sonenberg, Claudiu C. Gradinaru, Julie D. Forman-Kay

Publikováno v: Nature Communications, Vol 11, Iss 1, Pp 1-18 (2020)

Phosphorylation of eIF4E binding proteins (4E-BPs) controls their folding and regulates cap-dependent translation. Here, the authors show that phosphorylation of the C-terminal disordered region stabilizes the non-cooperatively folded 4E-BP domain to

Externí odkaz: https://doaj.org/article/57e3644d3e9b45b39d26e1a240848dcf

Pi-Pi contacts are an overlooked protein feature relevant to phase separation

Autor: Robert McCoy Vernon, Paul Andrew Chong, Brian Tsang, Tae Hun Kim, Alaji Bah, Patrick Farber, Hong Lin, Julie Deborah Forman-Kay

Publikováno v: eLife, Vol 7 (2018)

Protein phase separation is implicated in formation of membraneless organelles, signaling puncta and the nuclear pore. Multivalent interactions of modular binding domains and their target motifs can drive phase separation. However, forces promoting t

Externí odkaz: https://doaj.org/article/61b1e6c85e25468e8c6740116761c64f

O-Linked-N-Acetylglucosaminylation of the RNA-Binding Protein EWS N-Terminal Low Complexity Region Reduces Phase Separation and Enhances Condensate Dynamics

Autor: Jeffrey A. Toretsky, Hyun O Lee, Michael L Nosella, Iva Pritišanac, Julie D. Forman-Kay, P. Andrew Chong, Maria Tereshchenko

Publikováno v: Journal of the American Chemical Society. 143:11520-11534

Many membraneless organelles are thought to be biomolecular condensates formed by phase separation of proteins and other biopolymers. Post-translational modifications (PTMs) can impact protein phase separation behavior, although for many PTMs this as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f4d0021368f21baf3e65edf2481dfaac
https://doi.org/10.1021/jacs.1c04194

FUS-ALS mutants alter FMRP phase separation equilibrium and impair protein translation

Autor: Oscar G. Wilkins, Pietro Fratta, Seth Jarvis, Brian Tsang, Elizabeth M. C. Fisher, Cristian Bodo, Giampietro Schiavo, Maria Giovanna Garone, Anny Devoy, Gabriella Viero, Julie D. Forman-Kay, Micheal L. Nosella, P. Andrew Chong, Melis Pisiren, Agnieszka M. Ule, Nicol Birsa, Francesca Mattedi, Alessandro Rosa, Jack Humphrey, Rafaela Fernandez de la Fuente

Publikováno v: Science Advances
Science Advances 7 (2021). doi:10.1126/sciadv.abf8660
info:cnr-pdr/source/autori:Birsa N.; Ule A.M.; Garone M.G.; Tsang B.; Mattedi F.; Andrew Chong P.; Humphrey J.; Jarvis S.; Pisiren M.; Wilkins O.G.; Nosella M.L.; Devoy A.; Bodo C.; De la Fuente R.F.; Fisher E.M.C.; Rosa A.; Viero G.; Forman-Kay J.D.; Schiavo G.; Fratta P./titolo:FUS-ALS mutants alter FMRP phase separation equilibrium and impair protein translation/doi:10.1126%2Fsciadv.abf8660/rivista:Science Advances/anno:2021/pagina_da:/pagina_a:/intervallo_pagine:/volume:7

Cytoplasmic mislocalization of FUS-ALS mutants determines aberrant FMRP condensates and protein synthesis repression.
FUsed in Sarcoma (FUS) is a multifunctional RNA binding protein (RBP). FUS mutations lead to its cytoplasmic mislocalization an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cd61e34899281346ba403d1e869dc80
https://doi.org/10.1126/sciadv.abf8660

RGG/RG Motif Regions in RNA Binding and Phase Separation

Autor: P. Andrew Chong, Robert M. Vernon, Julie D. Forman-Kay

Publikováno v: Journal of molecular biology. 430(23)

RGG/RG motifs are RNA binding segments found in many proteins that can partition into membraneless organelles. They occur in the context of low-complexity disordered regions and often in multiple copies. Although short RGG/RG-containing regions can s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c917acf4370d42bb8c815d70730c4e43
https://pubmed.ncbi.nlm.nih.gov/29913160