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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

GRP78 protects a disintegrin and metalloprotease 17 against protein-disulfide isomerase A6 catalyzed inactivation

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Author(s):
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Schaefer, Miriam [1] ; Granato, Daniela C. [2] ; Krossa, Sebastian [3] ; Bartels, Anne-Kathrin [1] ; Yokoo, Sami [2] ; Dusterhoft, Stefan [4] ; Koudelka, Tomas [5] ; Scheidig, Axel J. [3] ; Tholey, Andreas [5] ; Paes Leme, Adriana F. [2] ; Groetzinger, Joachim [1] ; Lorenzen, Inken [1, 3]
Total Authors: 12
Affiliation:
[1] Univ Kiel, Inst Biochem, Olshausenstr 40, D-24118 Kiel - Germany
[2] CNPEM, LNBio, Lab Nacl Biociencias, Lab Espectrometria Massas, BR-13083970 Campinas, SP - Brazil
[3] Inst Zool, Dept Biol Struct, Kiel - Germany
[4] Sir William Dunn Sch Pathol, Oxford - England
[5] Univ Kiel, Inst Expt Med, Div Systemat Proteome Res, Kiel - Germany
Total Affiliations: 5
Document type: Journal article
Source: FEBS Letters; v. 591, n. 21, p. 3567-3587, NOV 2017.
Web of Science Citations: 4
Abstract

The shedding of ectodomains is a crucial mechanism in many physiological and pathological events. A disintegrin and metalloprotease-17 (ADAM17) is a key sheddase involved in essential processes, such as development, regeneration, and immune defense. ADAM17 exists in two conformations which differ in their disulfide connection in the membrane-proximal domain (MPD). Protein-disulfide isomerases (PDIs) on the cell surface convert the open MPD into a rigid closed form, which corresponds to inactive ADAM17. ADAM17 is expressed in its open activatable form in the endoplasmic reticulum (ER) and consequently must be protected against ER-resident PDI activity. Here, we show that the chaperone 78-kDa glucose-regulated protein (GRP78) protects the MPD against PDI-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 inhibition. (AU)

FAPESP's process: 11/02267-9 - Identifying ADAM17 partners and mapping the domains responsible for its interaction with other proteins.
Grantee:Daniela Campos Granato
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 09/54067-3 - Acquisition of a mass spectrometer coupled to a liquid chromatography system for increasing the capacity to meet the needs of users and for making new technologies available in the Laboratory of Mass Spectrometry
Grantee:Adriana Franco Paes Leme
Support Opportunities: Multi-user Equipment Program
FAPESP's process: 10/19278-0 - Study of regulation of ADAMs in oral cancer
Grantee:Adriana Franco Paes Leme
Support Opportunities: Research Grants - Young Investigators Grants