PACS-1 contains distinct motifs for nuclear-cytoplasmic transport and interacts with the RNA-binding protein PTBP1 in the nucleus and cytosol

FEBS Letters

article

Steven M. Trothen¹  Rong Xuan Zang¹  Antony Lurie¹  Jimmy D. Dikeakos¹ 

[1] Department of Microbiology and Immunology, Schulich School of Medicine and Dentistry, University of Western Ontario

关键词: IPO5/KPNA1;    nuclear export signal;    nuclear localization signal;    nuclear transport;    PACS-1;    protein–protein interaction;    PTBP1;    RNA-binding protein;    XPO1;   

DOI  :  10.1002/1873-3468.14243

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphofurin acidic cluster sorting protein 1 (PACS-1) is canonically a cytosolic trafficking protein, yet recent reports have described nuclear roles for PACS-1. Herein, we sought to define the nuclear transport mechanism of PACS-1. We demonstrate that PACS-1 nucleocytoplasmic trafficking is dependent on its interaction with the nuclear transport receptors importin alpha 5 and exportin 1. PACS-1 nuclear entry and exit are defined by a nuclear localization signal (NLS, residues 311-318) and nuclear export signal (NES3, residues 366-375). Mutation of the PACS-1 NLS and NES3 altered the localization of a complex formed between PACS-1 and an RNA-binding protein, polypyrimidine tract-binding protein 1. Overall, we identify the nuclear localization mechanism of PACS-1 and highlight a potential role for PACS-1 in RNA-binding protein trafficking.

【 授权许可】

Unknown