Janusz Wiśniewski
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Janusz Wiśniewski has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Dariusz Rakus
Department of Molecular Physiology and Neurobiology, University of Wrocław, 50-335 Wrocław, Poland
1 shared publication - Jakub Barciszewski
Institute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznań, Poland
1 shared publication - Jakub Turlik
Department of Molecular Physiology and Neurobiology, Faculty of Biological Sciences, University of Wrocław, 50-335 Wrocław, Poland
1 shared publication - Karolina Baran
Department of Protein Engineering, Faculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland
1 shared publication - Mariusz Jaskolski
Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland
1 shared publication - Przemysław Duda
Department of Molecular Physiology and Neurobiology, University of Wrocław, 50-335 Wrocław, Poland
1 shared publication
Latest Publications
- Open Access
- 30 October 2022
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 23 (21) , 13198
High-Resolution Crystal Structure of Muscle Phosphoglycerate Mutase Provides Insight into Its Nuclear Import and Role
Phosphoglycerate mutase (PGAM) is a glycolytic enzyme converting 3-phosphoglycerate to 2-phosphoglycerate, which in mammalian cells is expressed in two isoforms: brain (PGAM1) and muscle (PGAM2). Recently, it was shown that besides its enzymatic function, PGAM2 can be imported to the cell nucleus where it co-localizes with the nucleoli. It was suggested that it functions there to stabilize the nucleolar structure, maintain mRNA expression, and assist in the assembly of new pre-ribosomal subunits. However, the precise mechanism by which the protein translocates to the nucleus is unknown. In this study, we present the first crystal structure of PGAM2, identify the residues involved in the nuclear localization of the protein and propose that PGAM contains a “quaternary nuclear localization sequence (NLS)”, i.e., one that consists of residues from different protein chains. Additionally, we identify potential interaction partners for PGAM2 in the nucleoli and demonstrate that 14-3-3ζ/δ is indeed an interaction partner of PGAM2 in the nucleus. We also present evidence that the insulin/IGF1–PI3K–Akt–mTOR signaling pathway is responsible for the nuclear localization of PGAM2.
- 30 October 2022
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 23 (21) , 13198
Open AccessHigh-Resolution Crystal Structure of Muscle Phosphoglycerate Mutase Provides Insight into Its Nuclear Import and Role
Phosphoglycerate mutase (PGAM) is a glycolytic enzyme converting 3-phosphoglycerate to 2-phosphoglycerate, which in mammalian cells is expressed in two isoforms: brain (PGAM1) and muscle (PGAM2). Recently, it was shown that besides its enzymatic function, PGAM2 can be imported to the cell nucleus where it co-localizes with the nucleoli. It was suggested that it functions there to stabilize the nucleolar structure, maintain mRNA expression, and assist in the assembly of new pre-ribosomal subunits. However, the precise mechanism by which the protein translocates to the nucleus is unknown. In this study, we present the first crystal structure of PGAM2, identify the residues involved in the nuclear localization of the protein and propose that PGAM contains a “quaternary nuclear localization sequence (NLS)”, i.e., one that consists of residues from different protein chains. Additionally, we identify potential interaction partners for PGAM2 in the nucleoli and demonstrate that 14-3-3ζ/δ is indeed an interaction partner of PGAM2 in the nucleus. We also present evidence that the insulin/IGF1–PI3K–Akt–mTOR signaling pathway is responsible for the nuclear localization of PGAM2.