Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Phosphate-dependent nuclear export via a non-classical NES class recognized by exportin Msn5.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 2580, Year 2025
Publish date	Mar 16, 2025
Authors	Ho Yee Joyce Fung / Sanraj R Mittal / Ashley B Niesman / Jenny Jiou / Binita Shakya / Takuya Yoshizawa / Ahmet E Cansizoglu / Michael P Rout / Yuh Min Chook /
PubMed Abstract	Gene expression in response to environmental stimuli is dependent on nuclear localization of key signaling components, which can be tightly regulated by phosphorylation. This is exemplified by the ...Gene expression in response to environmental stimuli is dependent on nuclear localization of key signaling components, which can be tightly regulated by phosphorylation. This is exemplified by the phosphate-sensing transcription factor Pho4, which requires phosphorylation for nuclear export by the yeast exportin Msn5. Here, we present a high resolution cryogenic-electron microscopy structure showing the phosphorylated 35-residue nuclear export signal of Pho4, which binds the concave surface of Msn5 through two Pho4 phospho-serines that align with two Msn5 basic patches. These findings characterize a mechanism of phosphate-specific recognition mediated by a non-classical signal distinct from that for Exportin-1. Furthermore, the discovery that unliganded Msn5 is autoinhibited explains the positive cooperativity of Pho4/Ran-binding and proposes a mechanism for Pho4's release in the cytoplasm. These findings advance our understanding of the diversity of signals that drive nuclear export and how cargo phosphorylation is crucial in regulating nuclear transport and controlling cellular signaling pathways.
External links	Nat Commun / PubMed:40089503 / PubMed Central
Methods	EM (single particle)
Resolution	3.1 - 5.12 Å
Structure data	46548 9d43 EMDB-46548, PDB-9d43: Cryo-EM structure of unliganded yeast Exportin Msn5 Method: EM (single particle) / Resolution: 3.39 Å 46549 9d45 EMDB-46549, PDB-9d45: Cryo-EM structure of yeast Exportin Msn5 bound to cargo Pho4 and RanGTP Method: EM (single particle) / Resolution: 3.1 Å EMDB-46556: Cryo-EM Map of yeast Exportin Msn5 bound to cargo Pho4 and RanGTP (State 3-2) Method: EM (single particle) / Resolution: 3.23 Å EMDB-46557: Cryo-EM map of yeast Exportin Msn5 bound to cargo Pho4 and RanGTP (State 1-2) Method: EM (single particle) / Resolution: 3.37 Å EMDB-46560: Cryo-EM map of yeast Exportin Msn5 bound to cargo Pho4 and RanGTP (State 2-2) Method: EM (single particle) / Resolution: 3.33 Å EMDB-46561: Cryo-EM map of yeast Exportin Msn5 bound to cargo Pho4 (full-length) and RanGTP (State 3) Method: EM (single particle) / Resolution: 5.12 Å EMDB-46562: Cryo-EM map of yeast Exportin Msn5 bound to cargo Pho4 (full-length) and RanGTP (State 1) Method: EM (single particle) / Resolution: 4.91 Å 47291 9dxm EMDB-47291, PDB-9dxm: Cryo-EM structure of yeast Exportin Msn5 bound to RanGTP and Pho4 (not modeled) (State 2-1) Method: EM (single particle) / Resolution: 3.2 Å 47325 9dz6 EMDB-47325, PDB-9dz6: Cryo-EM structure of yeast Exportin Msn5 bound to RanGTP and Pho4 (not modeled) (State 3-1) Method: EM (single particle) / Resolution: 3.1 Å
Chemicals	ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying moleculeYM ChemComp-MG*: Unknown entry
Source	saccharomyces cerevisiae (brewer's yeast)
Keywords	TRANSPORT PROTEIN / Karyopherin / Exportin / Nuclear Export