Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer

Standard

Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer. / Wang, Yiyang; Fang, Shuai; Chen, Geng; Ganti, Rakhee; Chernova, Tatiana A.; Zhou, Li; Duong, Duc; Kiyokawa, Hiroaki; Li, Ming; Zhao, Bo; Shcherbik, Natalia; Chernoff, Yury O.; Yin, Jun.

In: Cell Chemical Biology, Vol. 28, No. 9, 8, 16.09.2021, p. 1283-1297.e8.

Research output: Contribution to journal › Article › peer-review

Harvard

Wang, Y, Fang, S, Chen, G, Ganti, R, Chernova, TA, Zhou, L, Duong, D, Kiyokawa, H, Li, M, Zhao, B, Shcherbik, N, Chernoff, YO & Yin, J 2021, 'Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer', Cell Chemical Biology, vol. 28, no. 9, 8, pp. 1283-1297.e8. https://doi.org/10.1016/j.chembiol.2021.02.005

APA

Wang, Y., Fang, S., Chen, G., Ganti, R., Chernova, T. A., Zhou, L., Duong, D., Kiyokawa, H., Li, M., Zhao, B., Shcherbik, N., Chernoff, Y. O., & Yin, J. (2021). Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer. Cell Chemical Biology, 28(9), 1283-1297.e8. [8]. https://doi.org/10.1016/j.chembiol.2021.02.005

Vancouver

Wang Y, Fang S, Chen G, Ganti R, Chernova TA, Zhou L et al. Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer. Cell Chemical Biology. 2021 Sep 16;28(9):1283-1297.e8. 8. https://doi.org/10.1016/j.chembiol.2021.02.005

Author

Wang, Yiyang ; Fang, Shuai ; Chen, Geng ; Ganti, Rakhee ; Chernova, Tatiana A. ; Zhou, Li ; Duong, Duc ; Kiyokawa, Hiroaki ; Li, Ming ; Zhao, Bo ; Shcherbik, Natalia ; Chernoff, Yury O. ; Yin, Jun. / Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer. In: Cell Chemical Biology. 2021 ; Vol. 28, No. 9. pp. 1283-1297.e8.

BibTeX

@article{3283e71ee24a429581926a516cee3cd1,

title = "Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer",

abstract = "Attachment of the ubiquitin (UB) peptide to proteins via the E1-E2-E3 enzymatic machinery regulates diverse biological pathways, yet identification of the substrates of E3 UB ligases remains a challenge. We overcame this challenge by constructing an “orthogonal UB transfer” (OUT) cascade with yeast E3 Rsp5 to enable the exclusive delivery of an engineered UB (xUB) to Rsp5 and its substrate proteins. The OUT screen uncovered new Rsp5 substrates in yeast, such as Pal1 and Pal2, which are partners of endocytic protein Ede1, and chaperones Hsp70-Ssb, Hsp82, and Hsp104 that counteract protein misfolding and control self-perpetuating amyloid aggregates (prions), resembling those involved in human amyloid diseases. We showed that prion formation and effect of Hsp104 on prion propagation are modulated by Rsp5. Overall, our work demonstrates the capacity of OUT to deconvolute the complex E3-substrate relationships in crucial biological processes such as endocytosis and protein assembly disorders through protein ubiquitination. We generated a substrate profile of yeast E3 ubiquitin ligase Rsp5 by following the exclusive transfer of an engineered xUB to Rsp5 substrates through an orthogonal ubiquitin transfer (OUT) cascade. Based on ubiquitination of disaggregase Hsp104 by Rsp5, we uncovered a role for Rsp5 in regulating prion formation and propagation.",

keywords = "amyloid, chaperone, endocytosis, Hsp104, protein engineering, Ssb, Sup35, ubiquitin ligase, yeast cell surface display, yeast prion, Saccharomyces cerevisiae Proteins/metabolism, Saccharomyces cerevisiae/enzymology, Endocytosis, Prions/metabolism, Ubiquitin-Protein Ligase Complexes/metabolism, Molecular Chaperones/metabolism, Endosomal Sorting Complexes Required for Transport/metabolism, Ubiquitin/metabolism, RIBOSOMAL-RNA, SACCHAROMYCES-CEREVISIAE, MESSENGER-RNA, GENE-EXPRESSION, HEXOSE TRANSPORTERS, RNA-POLYMERASE-II, CLATHRIN-MEDIATED ENDOCYTOSIS, PSI+ PRION, PROTEIN LIGASE, PROMOTER SYSTEM",

author = "Yiyang Wang and Shuai Fang and Geng Chen and Rakhee Ganti and Chernova, {Tatiana A.} and Li Zhou and Duc Duong and Hiroaki Kiyokawa and Ming Li and Bo Zhao and Natalia Shcherbik and Chernoff, {Yury O.} and Jun Yin",

year = "2021",

month = sep,

day = "16",

doi = "10.1016/j.chembiol.2021.02.005",

language = "English",

volume = "28",

pages = "1283--1297.e8",

journal = "Cell Chemical Biology",

issn = "2451-9448",

publisher = "Elsevier",

number = "9",

}

RIS

TY - JOUR

T1 - Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer

AU - Wang, Yiyang

AU - Fang, Shuai

AU - Chen, Geng

AU - Ganti, Rakhee

AU - Chernova, Tatiana A.

AU - Zhou, Li

AU - Duong, Duc

AU - Kiyokawa, Hiroaki

AU - Li, Ming

AU - Zhao, Bo

AU - Shcherbik, Natalia

AU - Chernoff, Yury O.

AU - Yin, Jun

PY - 2021/9/16

Y1 - 2021/9/16

N2 - Attachment of the ubiquitin (UB) peptide to proteins via the E1-E2-E3 enzymatic machinery regulates diverse biological pathways, yet identification of the substrates of E3 UB ligases remains a challenge. We overcame this challenge by constructing an “orthogonal UB transfer” (OUT) cascade with yeast E3 Rsp5 to enable the exclusive delivery of an engineered UB (xUB) to Rsp5 and its substrate proteins. The OUT screen uncovered new Rsp5 substrates in yeast, such as Pal1 and Pal2, which are partners of endocytic protein Ede1, and chaperones Hsp70-Ssb, Hsp82, and Hsp104 that counteract protein misfolding and control self-perpetuating amyloid aggregates (prions), resembling those involved in human amyloid diseases. We showed that prion formation and effect of Hsp104 on prion propagation are modulated by Rsp5. Overall, our work demonstrates the capacity of OUT to deconvolute the complex E3-substrate relationships in crucial biological processes such as endocytosis and protein assembly disorders through protein ubiquitination. We generated a substrate profile of yeast E3 ubiquitin ligase Rsp5 by following the exclusive transfer of an engineered xUB to Rsp5 substrates through an orthogonal ubiquitin transfer (OUT) cascade. Based on ubiquitination of disaggregase Hsp104 by Rsp5, we uncovered a role for Rsp5 in regulating prion formation and propagation.

AB - Attachment of the ubiquitin (UB) peptide to proteins via the E1-E2-E3 enzymatic machinery regulates diverse biological pathways, yet identification of the substrates of E3 UB ligases remains a challenge. We overcame this challenge by constructing an “orthogonal UB transfer” (OUT) cascade with yeast E3 Rsp5 to enable the exclusive delivery of an engineered UB (xUB) to Rsp5 and its substrate proteins. The OUT screen uncovered new Rsp5 substrates in yeast, such as Pal1 and Pal2, which are partners of endocytic protein Ede1, and chaperones Hsp70-Ssb, Hsp82, and Hsp104 that counteract protein misfolding and control self-perpetuating amyloid aggregates (prions), resembling those involved in human amyloid diseases. We showed that prion formation and effect of Hsp104 on prion propagation are modulated by Rsp5. Overall, our work demonstrates the capacity of OUT to deconvolute the complex E3-substrate relationships in crucial biological processes such as endocytosis and protein assembly disorders through protein ubiquitination. We generated a substrate profile of yeast E3 ubiquitin ligase Rsp5 by following the exclusive transfer of an engineered xUB to Rsp5 substrates through an orthogonal ubiquitin transfer (OUT) cascade. Based on ubiquitination of disaggregase Hsp104 by Rsp5, we uncovered a role for Rsp5 in regulating prion formation and propagation.

KW - amyloid

KW - chaperone

KW - endocytosis

KW - Hsp104

KW - protein engineering

KW - Ssb

KW - Sup35

KW - ubiquitin ligase

KW - yeast cell surface display

KW - yeast prion

KW - Saccharomyces cerevisiae Proteins/metabolism

KW - Saccharomyces cerevisiae/enzymology

KW - Endocytosis

KW - Prions/metabolism

KW - Ubiquitin-Protein Ligase Complexes/metabolism

KW - Molecular Chaperones/metabolism

KW - Endosomal Sorting Complexes Required for Transport/metabolism

KW - Ubiquitin/metabolism

KW - RIBOSOMAL-RNA

KW - SACCHAROMYCES-CEREVISIAE

KW - MESSENGER-RNA

KW - GENE-EXPRESSION

KW - HEXOSE TRANSPORTERS

KW - RNA-POLYMERASE-II

KW - CLATHRIN-MEDIATED ENDOCYTOSIS

KW - PSI+ PRION

KW - PROTEIN LIGASE

KW - PROMOTER SYSTEM

UR - http://www.scopus.com/inward/record.url?scp=85103090978&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/1eebb808-15de-3713-8645-21da281a48ba/

U2 - 10.1016/j.chembiol.2021.02.005

DO - 10.1016/j.chembiol.2021.02.005

M3 - Article

C2 - 33667410

AN - SCOPUS:85103090978

VL - 28

SP - 1283-1297.e8

JO - Cell Chemical Biology

JF - Cell Chemical Biology

SN - 2451-9448

IS - 9

M1 - 8

ER -

ID: 77118539