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Structural insight into the ZFAND1–p97 interaction involved in stress granule clearance

Lai, Chih-Hsuan ; Ko, Kuang-Ting ; Fan, Pei-Ju ; Yu, Tsun-Ai ; Chang, Chi-Fon ; Draczkowski, Piotr ; Hsu, Shang-Te Danny

The Journal of biological chemistry, 2024-05, Vol.300 (5), p.107230-107230, Article 107230 [Periódico revisado por pares]

United States: Elsevier Inc

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Título:
Structural insight into the ZFAND1–p97 interaction involved in stress granule clearance
Autor: Lai, Chih-Hsuan ; Ko, Kuang-Ting ; Fan, Pei-Ju ; Yu, Tsun-Ai ; Chang, Chi-Fon ; Draczkowski, Piotr ; Hsu, Shang-Te Danny
Assuntos: AlphaFold ; Arsenites - chemistry ; Arsenites - metabolism ; chemical cross-linking ; cryo-EM ; Crystallography, X-Ray ; dynamics ; Humans ; NMR spectroscopy ; p97 ; Protein Binding ; Protein Domains ; stress granule ; Stress Granules - chemistry ; Stress Granules - metabolism ; Ubiquitin - chemistry ; Ubiquitin - metabolism ; ubiquitin-like domain ; ubiquitin-proteasome system ; Valosin Containing Protein - chemistry ; Valosin Containing Protein - genetics ; Valosin Containing Protein - metabolism ; X-ray crystallography ; ZFAND1 ; zinc finger ; Zinc Fingers
É parte de: The Journal of biological chemistry, 2024-05, Vol.300 (5), p.107230-107230, Article 107230
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: Arsenite-induced stress granule (SG) formation can be cleared by the ubiquitin-proteasome system aided by the ATP-dependent unfoldase p97. ZFAND1 participates in this pathway by recruiting p97 to trigger SG clearance. ZFAND1 contains two An1-type zinc finger domains (ZF1 and ZF2), followed by a ubiquitin-like domain (UBL); but their structures are not experimentally determined. To shed light on the structural basis of the ZFAND1–p97 interaction, we determined the atomic structures of the individual domains of ZFAND1 by solution-state NMR spectroscopy and X-ray crystallography. We further characterized the interaction between ZFAND1 and p97 by methyl NMR spectroscopy and cryo-EM. 15N spin relaxation dynamics analysis indicated independent domain motions for ZF1, ZF2, and UBL. The crystal structure and NMR structure of UBL showed a conserved β-grasp fold homologous to ubiquitin and other UBLs. Nevertheless, the UBL of ZFAND1 contains an additional N-terminal helix that adopts different conformations in the crystalline and solution states. ZFAND1 uses the C-terminal UBL to bind to p97, evidenced by the pronounced line-broadening of the UBL domain during the p97 titration monitored by methyl NMR spectroscopy. ZFAND1 binding induces pronounced conformational heterogeneity in the N-terminal domain of p97, leading to a partial loss of the cryo-EM density of the N-terminal domain of p97. In conclusion, this work paved the way for a better understanding of the interplay between p97 and ZFAND1 in the context of SG clearance.
Editor: United States: Elsevier Inc
Idioma: Inglês

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Structural insight into the ZFAND1–p97 interaction involved in stress granule clearance

Lai, Chih-Hsuan ; Ko, Kuang-Ting ; Fan, Pei-Ju ; Yu, Tsun-Ai ; Chang, Chi-Fon ; Draczkowski, Piotr ; Hsu, Shang-Te Danny

United States: Elsevier Inc

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