The University of Southampton
University of Southampton Institutional Repository

FAM98A is a novel substrate of PRMT1 required for tumor cell migration, invasion, and colony formation

FAM98A is a novel substrate of PRMT1 required for tumor cell migration, invasion, and colony formation
FAM98A is a novel substrate of PRMT1 required for tumor cell migration, invasion, and colony formation
Protein arginine methylation, which is mediated by a family of protein arginine methyltransferases (PRMTs), is associated with numerous fundamental cellular processes. Accumulating studies have revealed that the expression of multiple PRMTs promotes cancer progression. In this study, we examined the role of PRMT1 in ovarian cancer cells. PRMT1 is expressed in multiple ovarian cancer cells, and the depletion of its expression suppressed colony formation, in vivo proliferation, migration, and invasion. To gain insight into PRMT1-mediated cancer progression, we searched for novel substrates of PRMT1. We found that FAM98A, whose physiological function is unknown, was arginine-methylated by PRMT1. FAM98A is expressed in numerous ovarian cancer cell lines and is important for the malignant characteristics of ovarian cancer cells. Our results indicate the possible role of the PRMT1-FAM98A pathway in cancer progression.
1010-4283
4531-4539
Akter, Khondker Ayesha
158fdaf8-1b26-4513-b123-f0e1729578b0
Mansour, Mohammed
03d901e1-959e-4c7d-acc6-33c6a4b129f7
Hyodo, Toshinori
d7721c0c-bfff-4899-b244-2686bfadd145
Ito, Satoko
1c0f236c-2128-41d0-8a88-00aaba826efb
Hamaguchi, Michinari
557c7853-d4ce-49b2-9069-6962047ed541
Senga, Takeshi
46e44e0d-98bf-459e-8afb-ee692cf14279
Akter, Khondker Ayesha
158fdaf8-1b26-4513-b123-f0e1729578b0
Mansour, Mohammed
03d901e1-959e-4c7d-acc6-33c6a4b129f7
Hyodo, Toshinori
d7721c0c-bfff-4899-b244-2686bfadd145
Ito, Satoko
1c0f236c-2128-41d0-8a88-00aaba826efb
Hamaguchi, Michinari
557c7853-d4ce-49b2-9069-6962047ed541
Senga, Takeshi
46e44e0d-98bf-459e-8afb-ee692cf14279

Akter, Khondker Ayesha, Mansour, Mohammed, Hyodo, Toshinori, Ito, Satoko, Hamaguchi, Michinari and Senga, Takeshi (2015) FAM98A is a novel substrate of PRMT1 required for tumor cell migration, invasion, and colony formation. Tumor Biology, 37 (4), 4531-4539. (doi:10.1007/s13277-015-4310-5).

Record type: Article

Abstract

Protein arginine methylation, which is mediated by a family of protein arginine methyltransferases (PRMTs), is associated with numerous fundamental cellular processes. Accumulating studies have revealed that the expression of multiple PRMTs promotes cancer progression. In this study, we examined the role of PRMT1 in ovarian cancer cells. PRMT1 is expressed in multiple ovarian cancer cells, and the depletion of its expression suppressed colony formation, in vivo proliferation, migration, and invasion. To gain insight into PRMT1-mediated cancer progression, we searched for novel substrates of PRMT1. We found that FAM98A, whose physiological function is unknown, was arginine-methylated by PRMT1. FAM98A is expressed in numerous ovarian cancer cell lines and is important for the malignant characteristics of ovarian cancer cells. Our results indicate the possible role of the PRMT1-FAM98A pathway in cancer progression.

This record has no associated files available for download.

More information

e-pub ahead of print date: 27 October 2015

Identifiers

Local EPrints ID: 432624
URI: http://eprints.soton.ac.uk/id/eprint/432624
ISSN: 1010-4283
PURE UUID: 589557b9-b5a6-475c-818f-cee6b66205fa

Catalogue record

Date deposited: 22 Jul 2019 16:30
Last modified: 16 Mar 2024 02:51

Export record

Altmetrics

Contributors

Author: Khondker Ayesha Akter
Author: Mohammed Mansour
Author: Toshinori Hyodo
Author: Satoko Ito
Author: Michinari Hamaguchi
Author: Takeshi Senga

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×