Please use this identifier to cite or link to this item: https://doi.org/10.1096/fj.201800997
Title: Unraveling the role of aurora A beyond centrosomes and spindle assembly: implications in muscle differentiation
Authors: Dhanasekaran, Karthigeyan
Bose, Arnab
Rao, Vinay J
Boopathi, Ramachandran
Shankar, Shilpa Rani 
Rao, Vinay Kumar 
Swaminathan, Amrutha
Vasudevan, Madavan
Taneja, Reshma 
Kundu, Tapas K 
Keywords: Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
Biology
Cell Biology
Life Sciences & Biomedicine - Other Topics
E2F4
subcellular localization
gene network
KINASE-ACTIVITY
A KINASE
EXPRESSION
MYOD
TRANSCRIPTION
ACTIVATION
GROWTH
Issue Date: 1-Jan-2019
Publisher: FEDERATION AMER SOC EXP BIOL
Citation: Dhanasekaran, Karthigeyan, Bose, Arnab, Rao, Vinay J, Boopathi, Ramachandran, Shankar, Shilpa Rani, Rao, Vinay Kumar, Swaminathan, Amrutha, Vasudevan, Madavan, Taneja, Reshma, Kundu, Tapas K (2019-01-01). Unraveling the role of aurora A beyond centrosomes and spindle assembly: implications in muscle differentiation. FASEB JOURNAL 33 (1) : 219-230. ScholarBank@NUS Repository. https://doi.org/10.1096/fj.201800997
Abstract: © The Author(s). Aurora kinases are critical mitotic serine/threonine kinases and are often implicated in tumorigenesis. Recent studies of the interphase functions for aurora kinase (Aurk)A have considerably expanded our understanding of its role beyond mitosis. To identify the unknown targets of AurkA, we used peptide array-based screening and found E2F4 to be a novel substrate. Phosphorylation of E2F4 by AurkA at Ser75 regulates its DNA binding and subcellular localization. Because E2F4 plays an important role in skeletal muscle differentiation, we attempted to gain insight into E2F4 phosphorylation in this context. We observed that a block in E2F4 phosphorylation retained it betterwithin the nucleus and inhibitedmuscle differentiation.RNAsequencing analysis revealed a perturbation of the gene network involved in the process ofmuscle differentiation andmitochondrial biogenesis. Collectively, our findings establish a novel role of AurkA in the process of skeletal muscle differentiation.
Source Title: FASEB JOURNAL
URI: https://scholarbank.nus.edu.sg/handle/10635/155218
ISSN: 0892-6638
1530-6860
DOI: 10.1096/fj.201800997
Appears in Collections:Staff Publications
Elements

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
FASEB preprint.pdf2.66 MBAdobe PDF

OPEN

Pre-printView/Download

Page view(s)

64
checked on Oct 10, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.