Yb-1 phosphorylation at serine 209 inhibits its nuclear translocation

Ekaterina M. Sogorina; Ekaterina R. Kim; Alexey V. Sorokin; Dmitry N. Lyabin; Lev P. Ovchinnikov; Daria A. Mordovkina; Irina A. Eliseeva

doi:10.3390/ijms23010428

Yb-1 phosphorylation at serine 209 inhibits its nuclear translocation

Ekaterina M. Sogorina, Ekaterina R. Kim, Alexey V. Sorokin, Dmitry N. Lyabin, Lev P. Ovchinnikov, Daria A. Mordovkina, Irina A. Eliseeva

GI Medical Oncology

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

YB-1 is a multifunctional DNA-and RNA-binding protein involved in cell proliferation, differentiation, and migration. YB-1 is a predominantly cytoplasmic protein that is transported to the nucleus in certain conditions, including DNA-damaging stress, transcription inhibition, and viral infection. In tumors, YB-1 nuclear localization correlates with high aggressiveness, multidrug resistance, and a poor prognosis. It is known that posttranslational modifications can regulate the nuclear translocation of YB-1. In particular, well-studied phosphorylation at serine 102 (S102) activates YB-1 nuclear import. Here, we report that Akt kinase phosphorylates YB-1 in vitro at serine 209 (S209), which is located in the vicinity of the YB-1 nuclear localization signal. Using phosphomimetic substitutions, we showed that S209 phosphorylation inhibits YB-1 nuclear translocation and prevents p-S102-mediated YB-1 nuclear import.

Original language	English (US)
Article number	428
Journal	International journal of molecular sciences
Volume	23
Issue number	1
DOIs	https://doi.org/10.3390/ijms23010428
State	Published - Jan 1 2022

Keywords

Akt
Nuclear transport
Phosphorylation
S102
S209
YB-1

ASJC Scopus subject areas

Catalysis
Molecular Biology
Spectroscopy
Computer Science Applications
Physical and Theoretical Chemistry
Organic Chemistry
Inorganic Chemistry

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10.3390/ijms23010428

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title = "Yb-1 phosphorylation at serine 209 inhibits its nuclear translocation",

abstract = "YB-1 is a multifunctional DNA-and RNA-binding protein involved in cell proliferation, differentiation, and migration. YB-1 is a predominantly cytoplasmic protein that is transported to the nucleus in certain conditions, including DNA-damaging stress, transcription inhibition, and viral infection. In tumors, YB-1 nuclear localization correlates with high aggressiveness, multidrug resistance, and a poor prognosis. It is known that posttranslational modifications can regulate the nuclear translocation of YB-1. In particular, well-studied phosphorylation at serine 102 (S102) activates YB-1 nuclear import. Here, we report that Akt kinase phosphorylates YB-1 in vitro at serine 209 (S209), which is located in the vicinity of the YB-1 nuclear localization signal. Using phosphomimetic substitutions, we showed that S209 phosphorylation inhibits YB-1 nuclear translocation and prevents p-S102-mediated YB-1 nuclear import.",

keywords = "Akt, Nuclear transport, Phosphorylation, S102, S209, YB-1",

author = "Sogorina, {Ekaterina M.} and Kim, {Ekaterina R.} and Sorokin, {Alexey V.} and Lyabin, {Dmitry N.} and Ovchinnikov, {Lev P.} and Mordovkina, {Daria A.} and Eliseeva, {Irina A.}",

note = "Publisher Copyright: {\textcopyright} 2021 by the authors. Licensee MDPI, Basel, Switzerland.",

year = "2022",

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doi = "10.3390/ijms23010428",

language = "English (US)",

volume = "23",

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T1 - Yb-1 phosphorylation at serine 209 inhibits its nuclear translocation

AU - Sogorina, Ekaterina M.

AU - Kim, Ekaterina R.

AU - Sorokin, Alexey V.

AU - Lyabin, Dmitry N.

AU - Ovchinnikov, Lev P.

AU - Mordovkina, Daria A.

AU - Eliseeva, Irina A.

PY - 2022/1/1

Y1 - 2022/1/1

N2 - YB-1 is a multifunctional DNA-and RNA-binding protein involved in cell proliferation, differentiation, and migration. YB-1 is a predominantly cytoplasmic protein that is transported to the nucleus in certain conditions, including DNA-damaging stress, transcription inhibition, and viral infection. In tumors, YB-1 nuclear localization correlates with high aggressiveness, multidrug resistance, and a poor prognosis. It is known that posttranslational modifications can regulate the nuclear translocation of YB-1. In particular, well-studied phosphorylation at serine 102 (S102) activates YB-1 nuclear import. Here, we report that Akt kinase phosphorylates YB-1 in vitro at serine 209 (S209), which is located in the vicinity of the YB-1 nuclear localization signal. Using phosphomimetic substitutions, we showed that S209 phosphorylation inhibits YB-1 nuclear translocation and prevents p-S102-mediated YB-1 nuclear import.

AB - YB-1 is a multifunctional DNA-and RNA-binding protein involved in cell proliferation, differentiation, and migration. YB-1 is a predominantly cytoplasmic protein that is transported to the nucleus in certain conditions, including DNA-damaging stress, transcription inhibition, and viral infection. In tumors, YB-1 nuclear localization correlates with high aggressiveness, multidrug resistance, and a poor prognosis. It is known that posttranslational modifications can regulate the nuclear translocation of YB-1. In particular, well-studied phosphorylation at serine 102 (S102) activates YB-1 nuclear import. Here, we report that Akt kinase phosphorylates YB-1 in vitro at serine 209 (S209), which is located in the vicinity of the YB-1 nuclear localization signal. Using phosphomimetic substitutions, we showed that S209 phosphorylation inhibits YB-1 nuclear translocation and prevents p-S102-mediated YB-1 nuclear import.

KW - Akt

KW - Nuclear transport

KW - Phosphorylation

KW - S102

KW - S209

KW - YB-1

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DO - 10.3390/ijms23010428

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C2 - 35008856

AN - SCOPUS:85122034706

SN - 1661-6596

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JO - International journal of molecular sciences

JF - International journal of molecular sciences

IS - 1

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ER -

Yb-1 phosphorylation at serine 209 inhibits its nuclear translocation

Abstract

Keywords

ASJC Scopus subject areas

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