NDLI: Phospho-ubiquitin-PARK2 complex as a marker for mitophagy defects

Please wait, while we are loading the content...

Phospho-ubiquitin-PARK2 complex as a marker for mitophagy defects

Content Provider	Scilit
Author	Callegari, Sylvie Oeljeklaus, Silke Warscheid, Bettina Dennerlein, Sven Thumm, Michael Rehling, Peter Dudek, Jan
Copyright Year	2017
Description	The E3 ubiquitin ligase PARK2 and the mitochondrial protein kinase PINK1 are required for the initiation of mitochondrial damage-induced mitophagy. Together, PARK2 and PINK1 generate a phospho-ubiquitin signal on outer mitochondrial membrane proteins that triggers recruitment of the autophagy machinery. This paper describes the detection of a defined 500-kDa phospho-ubiquitin-rich PARK2 complex that accumulates on mitochondria upon treatment with the membrane uncoupler CCCP. Formation of this complex is dependent on the presence of PINK1 and is absent in mutant forms of PARK2, whereby mitophagy is also arrested. These results signify a functional signaling complex that is essential for the progression of mitophagy. The visualization of the PARK2 signaling complex represents a novel marker for this critical step in mitophagy and can be used to monitor mitophagy progression in PARK2 mutants and to uncover additional upstream factors required for PARK2-mediated mitophagy signaling.
Related Links	https://www.tandfonline.com/doi/pdf/10.1080/15548627.2016.1254852?needAccess=true https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5240832/pdf
Ending Page	211
Page Count	11
Starting Page	201
ISSN	15548627
e-ISSN	15548635
DOI	10.1080/15548627.2016.1254852
Journal	Autophagy
Issue Number	1
Volume Number	13
Language	English
Publisher	Informa UK Limited
Publisher Date	2017-01-02
Access Restriction	Open
Subject Keyword	Cell Biology Autophagy E3 Ubiquitin Ligase Mitochondria Mitophagy Parkin Parkinson Disease Phospho-ubiquitin
Content Type	Text
Subject	Cell Biology Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The PINK1 p.I368N mutation affects protein stability and ubiquitin kinase activity

Parkin Mono-ubiquitinates Bcl-2 and Regulates Autophagy

Parkin recruitment to impaired mitochondria for nonselective ubiquitylation is facilitated by MITOL.

Temporal dynamics of PARK2/parkin and OPTN/optineurin recruitment during the mitophagy of damaged mitochondria

Site-specific Interaction Mapping of Phosphorylated Ubiquitin to Uncover Parkin Activation

Disease relevance of phosphorylated ubiquitin (p-S65-Ub)

The PARK2/Parkin receptor on damaged mitochondria revisited—uncovering the role of phosphorylated ubiquitin chains

The TOMM machinery is a molecular switch in PINK1 and PARK2/PARKIN-dependent mitochondrial clearance

The E3 Ubiquitin Ligase Parkin Is Recruited to the 26 S Proteasome via the Proteasomal Ubiquitin Receptor Rpn13

Phospho-ubiquitin-PARK2 complex as a marker for mitophagy defects

Similar Documents

The PINK1 p.I368N mutation affects protein stability and ubiquitin kinase activity

Parkin Mono-ubiquitinates Bcl-2 and Regulates Autophagy

Parkin recruitment to impaired mitochondria for nonselective ubiquitylation is facilitated by MITOL.

Temporal dynamics of PARK2/parkin and OPTN/optineurin recruitment during the mitophagy of damaged mitochondria

Site-specific Interaction Mapping of Phosphorylated Ubiquitin to Uncover Parkin Activation

Disease relevance of phosphorylated ubiquitin (p-S65-Ub)

The PARK2/Parkin receptor on damaged mitochondria revisited—uncovering the role of phosphorylated ubiquitin chains

The TOMM machinery is a molecular switch in PINK1 and PARK2/PARKIN-dependent mitochondrial clearance

The E3 Ubiquitin Ligase Parkin Is Recruited to the 26 S Proteasome via the Proteasomal Ubiquitin Receptor Rpn13

Phospho-ubiquitin-PARK2 complex as a marker for mitophagy defects