GGTase3 is a newly identified geranylgeranyltransferase targeting a ubiquitin ligase.


Journal

Nature structural & molecular biology
ISSN: 1545-9985
Titre abrégé: Nat Struct Mol Biol
Pays: United States
ID NLM: 101186374

Informations de publication

Date de publication:
07 2019
Historique:
received: 27 01 2019
accepted: 10 05 2019
pubmed: 19 6 2019
medline: 26 2 2020
entrez: 19 6 2019
Statut: ppublish

Résumé

Protein prenylation is believed to be catalyzed by three heterodimeric enzymes: FTase, GGTase1 and GGTase2. Here we report the identification of a previously unknown human prenyltransferase complex consisting of an orphan prenyltransferase α-subunit, PTAR1, and the catalytic β-subunit of GGTase2, RabGGTB. This enzyme, which we named GGTase3, geranylgeranylates FBXL2 to allow its localization at cell membranes, where this ubiquitin ligase mediates the polyubiquitylation of membrane-anchored proteins. In cells, FBXL2 is specifically recognized by GGTase3 despite having a typical carboxy-terminal CaaX prenylation motif that is predicted to be recognized by GGTase1. Our crystal structure analysis of the full-length GGTase3-FBXL2-SKP1 complex reveals an extensive multivalent interface specifically formed between the leucine-rich repeat domain of FBXL2 and PTAR1, which unmasks the structural basis of the substrate-enzyme specificity. By uncovering a missing prenyltransferase and its unique mode of substrate recognition, our findings call for a revision of the 'prenylation code'.

Identifiants

pubmed: 31209342
doi: 10.1038/s41594-019-0249-3
pii: 10.1038/s41594-019-0249-3
pmc: PMC6609460
mid: NIHMS1529146
doi:

Substances chimiques

F-Box Proteins 0
FBXL2 protein, human 0
Protein Subunits 0
Polyubiquitin 120904-94-1
Alkyl and Aryl Transferases EC 2.5.-
RABGGTB protein, human EC 2.5.-
Dimethylallyltranstransferase EC 2.5.1.1
PTAR1 protein, human EC 2.5.1.1

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

628-636

Subventions

Organisme : NCI NIH HHS
ID : R01 CA076584
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM057587
Pays : United States

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Auteurs

Shafi Kuchay (S)

Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY, USA.
Howard Hughes Medical Institute, New York University School of Medicine, New York, NY, USA.
Perlmutter NYU Cancer Center, New York University School of Medicine, New York, NY, USA.
Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL, USA.

Hui Wang (H)

Department of Pharmacology, University of Washington, Seattle, WA, USA.
Howard Hughes Medical Institute, University of Washington, Seattle, WA, USA.

Antonio Marzio (A)

Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY, USA.
Perlmutter NYU Cancer Center, New York University School of Medicine, New York, NY, USA.

Kunj Jain (K)

Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY, USA.
Perlmutter NYU Cancer Center, New York University School of Medicine, New York, NY, USA.

Harrison Homer (H)

Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY, USA.
Perlmutter NYU Cancer Center, New York University School of Medicine, New York, NY, USA.

Nicole Fehrenbacher (N)

Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY, USA.
Perlmutter NYU Cancer Center, New York University School of Medicine, New York, NY, USA.

Mark R Philips (MR)

Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY, USA.
Perlmutter NYU Cancer Center, New York University School of Medicine, New York, NY, USA.

Ning Zheng (N)

Department of Pharmacology, University of Washington, Seattle, WA, USA. nzheng@uw.edu.
Howard Hughes Medical Institute, University of Washington, Seattle, WA, USA. nzheng@uw.edu.

Michele Pagano (M)

Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY, USA. michele.pagano@nyumc.org.
Howard Hughes Medical Institute, New York University School of Medicine, New York, NY, USA. michele.pagano@nyumc.org.
Perlmutter NYU Cancer Center, New York University School of Medicine, New York, NY, USA. michele.pagano@nyumc.org.

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Classifications MeSH