2017•OncotargetOpen access

Nucleocytoplasmic shuttling of SOX14A and SOX14B transcription factors

Zhen‐Yu She, Wan‐Xi Yang

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Abstract

// Zhen-Yu She 1 and Wan-Xi Yang 1 1 The Sperm Laboratory, College of Life Sciences, Zhejiang University, Hangzhou 310058, China Correspondence to: Wan-Xi Yang, email: wxyang@spermlab.org Keywords: SOX14, HMG box, nuclear localization signal, nuclear transport, nuclear export Received: November 23, 2016 Accepted: January 11, 2017 Published: February 07, 2017 Abstract The nucleocytoplasmic shuttling of SOX transcription factors play a crucial role in the regulation of SOX protein functions during development. In this study, we have demonstrated two nuclear localization signals in the HMG box of Eriocheir sinensis SOX14A and SOX14B. These two conserved nuclear localization signals mediate nuclear transport. The N-termini nuclear localization signal mediates the calmodulin-dependent pathway and the C-termini nuclear localization signal interacts with the importin-β pathway. The targeted deletion of nuclear localization signals of SOX14A/B dramatically inhibits the nuclear accumulation. We have first time revealed a non-classic nuclear export signal in the HMG box of E. sinensis SOX14A/B proteins is responds to leptomycin B. E. sinensis SOX14A/B is transported from the nucleus to the cytoplasm via a CRM1-dependent nuclear export pathway. And E. sinensis SOX14A/B are not belong to the subgroup E SOX proteins. Furthermore, these findings could shed a light on the mechanisms involved in the nuclear export of SOX proteins. The imperfect nuclear export signal on other SOX proteins, rather than just those of the SOXE group, may also be functional for nuclear export.

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// Zhen-Yu She 1 and Wan-Xi Yang 1 1 The Sperm Laboratory, College of Life Sciences, Zhejiang University, Hangzhou 310058, China Correspondence to: Wan-Xi Yang, email: wxyang@spermlab.org Keywords: SOX14, HMG box, nuclear localization signal, nuclear transport, nuclear export Received: November 23, 2016 Accepted: January 11, 2017 Published: February 07, 2017 Abstract The nucleocytoplasmic shuttling of SOX transcription factors play a crucial role in the regulation of SOX protein functions during development. In this study, we have demonstrated two nuclear localization signals in the HMG box of Eriocheir sinensis SOX14A and SOX14B. These two conserved nuclear localization signals mediate nuclear transport. The N-termini nuclear localization signal mediates the calmodulin-dependent pathway and the C-termini nuclear localization signal interacts with the importin-β pathway. The targeted deletion of nuclear localization signals of SOX14A/B dramatically inhibits the nuclear accumulation. We have first time revealed a non-classic nuclear export signal in the HMG box of E. sinensis SOX14A/B proteins is responds to leptomycin B. E. sinensis SOX14A/B is transported from the nucleus to the cytoplasm via a CRM1-dependent nuclear export pathway. And E. sinensis SOX14A/B are not belong to the subgroup E SOX proteins. Furthermore, these findings could shed a light on the mechanisms involved in the nuclear export of SOX proteins. The imperfect nuclear export signal on other SOX proteins, rather than just those of the SOXE group, may also be functional for nuclear export.

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Available abstract

// Zhen-Yu She 1 and Wan-Xi Yang 1 1 The Sperm Laboratory, College of Life Sciences, Zhejiang University, Hangzhou 310058, China Correspondence to: Wan-Xi Yang, email: wxyang@spermlab.org Keywords: SOX14, HMG box, nuclear localization signal, nuclear transport, nuclear export Received: November 23, 2016 Accepted: January 11, 2017 Published: February 07, 2017 Abstract The nucleocytoplasmic shuttling of SOX transcription factors play a crucial role in the regulation of SOX protein functions during development. In this study, we have demonstrated two nuclear localization signals in the HMG box of Eriocheir sinensis SOX14A and SOX14B. These two conserved nuclear localization signals mediate nuclear transport. The N-termini nuclear localization signal mediates the calmodulin-dependent pathway and the C-termini nuclear localization signal interacts with the importin-β pathway. The targeted deletion of nuclear localization signals of SOX14A/B dramatically inhibits the nuclear accumulation. We have first time revealed a non-classic nuclear export signal in the HMG box of E. sinensis SOX14A/B proteins is responds to leptomycin B. E. sinensis SOX14A/B is transported from the nucleus to the cytoplasm via a CRM1-dependent nuclear export pathway. And E. sinensis SOX14A/B are not belong to the subgroup E SOX proteins. Furthermore, these findings could shed a light on the mechanisms involved in the nuclear export of SOX proteins. The imperfect nuclear export signal on other SOX proteins, rather than just those of the SOXE group, may also be functional for nuclear export.

Key concepts: Nuclear export signal, Nuclear transport, Nuclear localization sequence, Importin, Cell biology, Nuclear protein, Transcription factor, Nucleoporin

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