• Mechanism of an ATP-independent Protein Disaggregase: II. Distinct molecular interactions drive multiple steps during aggregate disassembly

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Metadata

Document Title

Mechanism of an ATP-independent Protein Disaggregase: II. Distinct molecular interactions drive multiple steps during aggregate disassembly

Author

Jaru-Ampornpan P., Liang F.-C., Nisthal A., Nguyen T.X., Wang P., Shen K., Mayo S.L., Shan S.-O.

Name from Authors Collection

Jaru-Ampornpan P.

Scopus Author ID

16744130800

ORCID ID

NULL

|

Liang F.-C.

Scopus Author ID

35170136900

ORCID ID

NULL

|

Nisthal A.

Scopus Author ID

24385408200

ORCID ID

NULL

|

Nguyen T.X.

Scopus Author ID

55473731500

ORCID ID

NULL

|

Wang P.

Scopus Author ID

55696384800

ORCID ID

NULL

|

Shen K.

Scopus Author ID

57213547445

ORCID ID

NULL

|

Mayo S.L.

Scopus Author ID

7006470104

ORCID ID

NULL

|

Shan S.-O.

Scopus Author ID

7005052558

ORCID ID

NULL

Affiliations

Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 E. California Blvd., Pasadena, CA 91125, United States; Division of Biology, California Institute of Technology, Pasadena, CA 91125, United States; Agricultural Biotechnology Research Unit, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathum Thani 12120, Thailand

Type

Article

Source Title

Journal of Biological Chemistry

ISSN

00219258

Year

2013

Volume

288

Issue

19

Page

13431-13445

Open Access

Hybrid Gold, Green

DOI

10.1074/jbc.M113.462861

Format

PDF

Abstract

Background: A novel chaperone, cpSRP43, disassembles a family of membrane protein aggregates. Results: cpSRP43-mediated disaggregation requires two steps, recognition and remodeling, each with distinct molecular requirements. Conclusion: cpSRP43 uses distinct substrate binding interactions to recognize and then remodel and disrupt the protein aggregate. Significance: Mechanism of this novel ATP-independent disaggregase guides the understanding of analogous systems and design efforts to target protein aggregates of interest. Copyright © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

License

CC BY

Rights

ASBMB

Publication Source

Scopus

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