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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.

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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

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Date deposited: 22 Jul 2019 16:30
Last modified: 22 Jul 2019 16:30

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Contributors

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

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