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TitleAKIRIN2 controls the nuclear import of proteasomes in vertebrates.
Journal, issue, pagesNature, Vol. 599, Issue 7885, Page 491-496, Year 2021
Publish dateOct 28, 2021
AuthorsMelanie de Almeida / Matthias Hinterndorfer / Hanna Brunner / Irina Grishkovskaya / Kashish Singh / Alexander Schleiffer / Julian Jude / Sumit Deswal / Robert Kalis / Milica Vunjak / Thomas Lendl / Richard Imre / Elisabeth Roitinger / Tobias Neumann / Susanne Kandolf / Michael Schutzbier / Karl Mechtler / Gijs A Versteeg / David Haselbach / Johannes Zuber /
PubMed AbstractProtein expression and turnover are controlled through a complex interplay of transcriptional, post-transcriptional and post-translational mechanisms to enable spatial and temporal regulation of ...Protein expression and turnover are controlled through a complex interplay of transcriptional, post-transcriptional and post-translational mechanisms to enable spatial and temporal regulation of cellular processes. To systematically elucidate such gene regulatory networks, we developed a CRISPR screening assay based on time-controlled Cas9 mutagenesis, intracellular immunostaining and fluorescence-activated cell sorting that enables the identification of regulatory factors independent of their effects on cellular fitness. We pioneered this approach by systematically probing the regulation of the transcription factor MYC, a master regulator of cell growth. Our screens uncover a highly conserved protein, AKIRIN2, that is essentially required for nuclear protein degradation. We found that AKIRIN2 forms homodimers that directly bind to fully assembled 20S proteasomes to mediate their nuclear import. During mitosis, proteasomes are excluded from condensing chromatin and re-imported into newly formed daughter nuclei in a highly dynamic, AKIRIN2-dependent process. Cells undergoing mitosis in the absence of AKIRIN2 become devoid of nuclear proteasomes, rapidly causing accumulation of MYC and other nuclear proteins. Collectively, our study reveals a dedicated pathway controlling the nuclear import of proteasomes in vertebrates and establishes a scalable approach to decipher regulators in essential cellular processes.
External linksNature / PubMed:34711951
MethodsEM (single particle)
Resolution3.2 - 21.0 Å
Structure data

EMDB-11649:
Akirin2 bound to the human 26S proteasome
Method: EM (single particle) / Resolution: 21.0 Å

12341

7nht

EMDB-12341, PDB-7nht:
Akirin2 bound human proteasome
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-K:
Unknown entry

Source
  • homo sapiens (human)
  • Human (human)
KeywordsTRANSPORT PROTEIN / proteasome / nuclear import

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