DNA damage response signaling does not trigger redistribution of SAMHD1 to nuclear foci

Author(s)

Medeiros, Ana Carla ^[1] ; Soares, Claudia S. ^[1] ; Coelho, Priscila O. ^[1] ; Vieira, Nichelle A. ^[1] ; Baqui, Munira M. A. ^{[1, 2]} ; Teixeira, Felipe R. ^{[1, 3, 4]} ; Gomes, Marcelo D. ^[1]

Affiliation

^[1] Univ Sao Paulo, Ribeirao Preto Med Sch, Dept Biochem & Immunol, Ave Bandeirantes 3900, BR-14049900 Ribeirao Preto, SP - Brazil

^[2] Univ Sao Paulo, Ribeirao Preto Med Sch, Dept Cell Biol, Ribeirao Preto - Brazil

^[3] Univ Sao Paulo, Ribeirao Preto Med Sch, Ribeirao Preto - Brazil

^[4] Univ Fed Sao Carlos, Dept Genet & Evolut, Sao Carlos, SP - Brazil

• Document type: Journal article
• Source: Biochemical and Biophysical Research Communications; v. 499, n. 4, p. 790-796, MAY 23 2018.
• Web of Science Citations: 1

Abstract

SAMHD1 (Sterile alpha motif and histidine-aspartic acid (HD) domain containing protein 1) is a deoxyribonucleoside triphosphate (dNTP) triphosphohydrolase (dNTPase) that restricts viral replication in infected cells. This protein is also involved in DNA repair by assisting in DNA end resection by homologous recombination (HR) after DNA double-strand break (DSB) induction with camptothecin (CPT) or etoposide (ETO). We showed that a monoclonal anti-SAMHD1 antibody produced against the full-length protein detected an unspecific 50 kDa protein that colocalized with dot-like structures after CPT treatment in HeLa cells. In contrast, a polyclonal anti-SAMHD1 antibody raised against the N-terminus of this protein specifically detected SAMHD1, as shown in Jurkat, HAP1(KO) and HEK293T SAMHD1-siRNA cell lysates compared with their respective controls. Our findings showed that SAMHD1 is not localized in dot-like structures under DSB induction in HeLa cells. (C) 2018 Elsevier Inc. All rights reserved. (AU)

• FAPESP's process: 14/10898-7 - High-throughput RNAi library screening to identify novel regulators of ERKs
• Grantee: Marcelo Damário Gomes
• Support Opportunities: Regular Research Grants
• FAPESP's process: 10/19435-9 - Identification of proteins that regulate nuclear structures rich in FBXO25 (FANDs) by GF-TAP
• Grantee: Cláudia Sossai Soares
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• FAPESP's process: 16/00792-2 - Functional characterization of the E3 ubiquitin-ligase SCF(Fbxo7/PARK15) in the oncogenic Wnt pathway and mitochondrial homeostasis
• Grantee: Felipe Roberti Teixeira
• Support Opportunities: Regular Research Grants