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Unique proline-rich domain regulates the chaperone function of AIPL1.
Biochemistry. 2013 Mar 26; 52(12):2089-96.B

Abstract

Human aryl hydrocarbon receptor (AHR) interacting protein (AIP) and AIP like 1 (AIPL1) are cochaperones of Hsp90 which share 49% sequence identity. Both proteins contain an N-terminal FKBP-like prolyl peptidyl isomerase (PPIase) domain followed by a tetratricopeptide repeat (TPR) domain. In addition, AIPL1 harbors a unique C-terminal proline-rich domain (PRD). Little is known about the functional relevance of the individual domains and how these contribute to the association with Hsp90. In this study, we show that these cochaperones differ from other Hsp90-associated PPIase as their FKBP domains are enzymatically inactive. Furthermore, in contrast to other large PPIases, AIP is inactive as a chaperone. AIPL1, however, exhibits chaperone activity and prevents the aggregation of non-native proteins. The unique proline-rich domain of AIPL1 is important for its chaperone function as its truncation severely affects the ability of AIPL1 to bind non-native proteins. Furthermore, the proline-rich domain decreased the affinity of AIPL1 for Hsp90, implying that this domain acts as a negative regulator of the Hsp90 interaction besides being necessary for efficient binding of AIPL1 to non-native proteins.

Authors+Show Affiliations

Center for Integrated Protein Science at the Department Chemie, Technische Universität München , Lichtenbergstrasse 4, D-85747 Garching, Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23418749

Citation

Li, Jing, et al. "Unique Proline-rich Domain Regulates the Chaperone Function of AIPL1." Biochemistry, vol. 52, no. 12, 2013, pp. 2089-96.
Li J, Zoldak G, Kriehuber T, et al. Unique proline-rich domain regulates the chaperone function of AIPL1. Biochemistry. 2013;52(12):2089-96.
Li, J., Zoldak, G., Kriehuber, T., Soroka, J., Schmid, F. X., Richter, K., & Buchner, J. (2013). Unique proline-rich domain regulates the chaperone function of AIPL1. Biochemistry, 52(12), 2089-96. https://doi.org/10.1021/bi301648q
Li J, et al. Unique Proline-rich Domain Regulates the Chaperone Function of AIPL1. Biochemistry. 2013 Mar 26;52(12):2089-96. PubMed PMID: 23418749.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Unique proline-rich domain regulates the chaperone function of AIPL1. AU - Li,Jing, AU - Zoldak,Gabriel, AU - Kriehuber,Thomas, AU - Soroka,Joanna, AU - Schmid,Franz X, AU - Richter,Klaus, AU - Buchner,Johannes, Y1 - 2013/03/13/ PY - 2013/2/20/entrez PY - 2013/2/20/pubmed PY - 2014/2/11/medline SP - 2089 EP - 96 JF - Biochemistry JO - Biochemistry VL - 52 IS - 12 N2 - Human aryl hydrocarbon receptor (AHR) interacting protein (AIP) and AIP like 1 (AIPL1) are cochaperones of Hsp90 which share 49% sequence identity. Both proteins contain an N-terminal FKBP-like prolyl peptidyl isomerase (PPIase) domain followed by a tetratricopeptide repeat (TPR) domain. In addition, AIPL1 harbors a unique C-terminal proline-rich domain (PRD). Little is known about the functional relevance of the individual domains and how these contribute to the association with Hsp90. In this study, we show that these cochaperones differ from other Hsp90-associated PPIase as their FKBP domains are enzymatically inactive. Furthermore, in contrast to other large PPIases, AIP is inactive as a chaperone. AIPL1, however, exhibits chaperone activity and prevents the aggregation of non-native proteins. The unique proline-rich domain of AIPL1 is important for its chaperone function as its truncation severely affects the ability of AIPL1 to bind non-native proteins. Furthermore, the proline-rich domain decreased the affinity of AIPL1 for Hsp90, implying that this domain acts as a negative regulator of the Hsp90 interaction besides being necessary for efficient binding of AIPL1 to non-native proteins. SN - 1520-4995 UR - https://www.unboundmedicine.com/medline/citation/23418749/Unique_proline_rich_domain_regulates_the_chaperone_function_of_AIPL1_ L2 - https://doi.org/10.1021/bi301648q DB - PRIME DP - Unbound Medicine ER -