PACS‐1 contains distinct motifs for nuclear‐cytoplasmic transport and interacts with the RNA‐binding protein PTBP1 in the nucleus and cytosol
| Autor: | Jimmy D. Dikeakos, Steven M. Trothen, Antony Lurie, Rong Xuan Zang |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
endocrine system diseases
education Biophysics RNA-binding protein Biochemistry 03 medical and health sciences XPO1 Cytosol 0302 clinical medicine Structural Biology Exportin-1 health services administration Genetics Nuclear export signal Molecular Biology 030304 developmental biology 0303 health sciences education.field_of_study Chemistry food and beverages Cell Biology PTBP1 humanities 3. Good health Cell biology 030220 oncology & carcinogenesis Phosphofurin acidic cluster sorting protein 1 Nuclear transport Nuclear localization sequence |
| Zdroj: | FEBS Letters. 596:232-248 |
| ISSN: | 1873-3468 0014-5793 |
| DOI: | 10.1002/1873-3468.14243 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text