Tyrosine phosphorylation regulates hnRNPA2 granule protein partitioning and reduces neurodegeneration-Reference-Cited by-同舟云学术

Tyrosine phosphorylation regulates hnRNPA2 granule protein partitioning and reduces neurodegeneration

Published:2020-12-22 Issue:3 Volume:40 Page:
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:EMBO J

Author:

Ryan Veronica H¹,Perdikari Theodora M²,Naik Mandar T³,Saueressig Camillo F⁴^ORCID,Lins Jeremy⁴,Dignon Gregory L⁵^ORCID,Mittal Jeetain⁵^ORCID,Hart Anne C⁴^ORCID,Fawzi Nicolas L³^ORCID

Affiliation:

1. Neuroscience Graduate ProgramBrown University Providence RI USA

2. Biomedical Engineering Graduate Program Brown University Providence RI USA

3. Department of Molecular Pharmacology, Physiology, and Biotechnology Brown University Providence RI USA

4. Department of Neuroscience Brown University Providence RI USA

5. Department of Chemical and Biomolecular Engineering Lehigh University Bethlehem PA USA

Funder

National Institute of General Medical Sciences

Division of Molecular and Cellular Biosciences

National Institute on Aging

U.S. Department of Energy

National Institute of Neurological Disorders and Stroke

Division of Materials Research

National Science Foundation

NIH Office of the Director

Publisher

EMBO

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Link

https://onlinelibrary.wiley.com/doi/pdf/10.15252/embj.2020105001

Reference83 articles.

1. Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes.

2. Axonal Transport of TDP-43 mRNA Granules Is Impaired by ALS-Causing Mutations

3. The SH3 domain of Fyn kinase interacts with and induces liquid–liquid phase separation of the low-complexity domain of hnRNPA2

4. Transient, Sparsely Populated Compact States of Apo and Calcium-Loaded Calmodulin Probed by Paramagnetic Relaxation Enhancement: Interplay of Conformational Selection and Induced Fit

5. A TOG:αβ-tubulin Complex Structure Reveals Conformation-Based Mechanisms for a Microtubule Polymerase

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