NDLI: Arabidopsis PIAL1 and 2 promote SUMO chain formation as E4-type SUMO ligases and are involved in stress responses and sulfur metabolism.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Tomanov, Konstantin Zeschmann, Anja Hermkes, Rebecca Eifler, Karolin Ziba, Ionida Grieco, Michele Novatchkova, Maria Hofmann, Kay Hesse, Holger Bachmair, Andreas
Description	Country affiliation: Austria Author Affiliation: Tomanov K ( Max F. Perutz Laboratories, Center for Molecular Biology of the University of Vienna, A-1030 Vienna, Austria.); Zeschmann A ( Department of Molecular Plant Physiology, Max Planck Institute for Molecular Plant Physiology, D-14476 Potsdam, Germany.); Hermkes R ( Department of Plant Developmental Biology, Max Planck Institute for Plant Breeding Research, D-50829 Cologne, Germany.); Eifler K ( Max F. Perutz Laboratories, Center for Molecular Biology of the University of Vienna, A-1030 Vienna, Austria Department of Plant Developmental Biology, Max Planck Institute for Plant Breeding Research, D-50829 Cologne, Germany.); Ziba I ( Max F. Perutz Laboratories, Center for Molecular Biology of the University of Vienna, A-1030 Vienna, Austria.); Grieco M ( Department of Ecogenomics and Systems Biology, University of Vienna, A-1090 Vienna, Austria.); Novatchkova M ( Research Institute of Molecular Pathology, A-1030 Vienna, Austria.); Hofmann K ( Institute for Genetics, University of Cologne, D-50674 Cologne, Germany.); Hesse H ( Department of Molecular Plant Physiology, Max Planck Institute for Molecular Plant Physiology, D-14476 Potsdam, Germany.); Bachmair A ( Max F. Perutz Laboratories, Center for Molecular Biology of the University of Vienna, A-1030 Vienna, Austria Department of Plant Developmental Biology, Max Planck Institute for Plant Breeding Research, D-50829 Cologne, Germany andreas.bachmair@univie.ac.at.)
Abstract	The Arabidopsis thaliana genes PROTEIN INHIBITOR OF ACTIVATED STAT LIKE1 (PIAL1) and PIAL2 encode proteins with SP-RING domains, which occur in many ligases of the small ubiquitin-related modifier (SUMO) conjugation pathway. We show that PIAL1 and PIAL2 function as SUMO ligases capable of SUMO chain formation and require the SUMO-modified SUMO-conjugating enzyme SCE1 for optimal activity. Mutant analysis indicates a role for PIAL1 and 2 in salt stress and osmotic stress responses, whereas under standard conditions, the mutants show close to normal growth. Mutations in PIAL1 and 2 also lead to altered sulfur metabolism. We propose that, together with SUMO chain binding ubiquitin ligases, these enzymes establish a pathway for proteolytic removal of sumoylation substrates.
File Format	HTM / HTML
ISSN	10404651
e-ISSN	1531298X
DOI	10.1105/tpc.114.131300
Journal	THE PLANT CELL ONLINE
Issue Number	11
Volume Number	26
Language	English
Publisher	American Society of Plant Biologists
Publisher Date	2014-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Botany Arabidopsis Proteins Metabolism Arabidopsis Enzymology Ubiquitin-conjugating Enzymes Ubiquitin-protein Ligases Ubiquitin Genetics Physiology Models, Molecular Mutagenesis, Insertional Phylogeny Seedling Stress, Physiological Sumoylation
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science

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

Arabidopsis PIAL1 and 2 promote SUMO chain formation as E4-type SUMO ligases and are involved in stress responses and sulfur metabolism: Correction

Arabidopsis PIAL1 and 2 Promote SUMO Chain Formation as E4-Type SUMO Ligases and Are Involved in Stress Responses and Sulfur Metabolism [C] [W] [OPEN]

Site-specific inhibition of the small ubiquitin-like modifier (SUMO)-conjugating enzyme Ubc9 selectively impairs SUMO chain formation

SUMO-targeted ubiquitin ligases $^{☆☆}$

Small ubiquitin-like modifier conjugating enzyme with active site mutation acts as dominant negative inhibitor of SUMO conjugation in arabidopsis(F).

Ubiquitination and SUMOylation of annexin A1 and helicase activity

Arabidopsis C3HC4-RING finger E3 ubiquitin ligase AtAIRP4 positively regulates stress-responsive abscisic acid signaling.

RWD Domain as an E2 (Ubc9)-Interaction Module.

MEL-18 Interacts with HSF2 and the SUMO E2 UBC9 to Inhibit HSF2 Sumoylation

Arabidopsis PIAL1 and 2 promote SUMO chain formation as E4-type SUMO ligases and are involved in stress responses and sulfur metabolism.

Similar Documents

Arabidopsis PIAL1 and 2 promote SUMO chain formation as E4-type SUMO ligases and are involved in stress responses and sulfur metabolism: Correction

Arabidopsis PIAL1 and 2 Promote SUMO Chain Formation as E4-Type SUMO Ligases and Are Involved in Stress Responses and Sulfur Metabolism [C] [W] [OPEN]

Site-specific inhibition of the small ubiquitin-like modifier (SUMO)-conjugating enzyme Ubc9 selectively impairs SUMO chain formation

SUMO-targeted ubiquitin ligases $^{☆☆}$

Small ubiquitin-like modifier conjugating enzyme with active site mutation acts as dominant negative inhibitor of SUMO conjugation in arabidopsis(F).

Ubiquitination and SUMOylation of annexin A1 and helicase activity

Arabidopsis C3HC4-RING finger E3 ubiquitin ligase AtAIRP4 positively regulates stress-responsive abscisic acid signaling.

RWD Domain as an E2 (Ubc9)-Interaction Module.

MEL-18 Interacts with HSF2 and the SUMO E2 UBC9 to Inhibit HSF2 Sumoylation

Arabidopsis PIAL1 and 2 promote SUMO chain formation as E4-type SUMO ligases and are involved in stress responses and sulfur metabolism.