MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission.

Abstract:

:The modification of proteins by the small ubiquitin-like modifier (SUMO) is known to regulate an increasing array of cellular processes. SUMOylation of the mitochondrial fission GTPase dynamin-related protein 1 (DRP1) stimulates mitochondrial fission, suggesting that SUMOylation has an important function in mitochondrial dynamics. The conjugation of SUMO to its substrates requires a regulatory SUMO E3 ligase; however, so far, none has been functionally associated with the mitochondria. By using biochemical assays, overexpression and RNA interference experiments, we characterized the mitochondrial-anchored protein ligase (MAPL) as the first mitochondrial-anchored SUMO E3 ligase. Furthermore, we show that DRP1 is a substrate for MAPL, providing a direct link between MAPL and the fission machinery. Importantly, the large number of unidentified mitochondrial SUMO targets suggests a global role for SUMOylation in mitochondrial function, placing MAPL as a crucial component in the regulation of multiple conjugation events.

journal_name

EMBO Rep

journal_title

EMBO reports

authors

Braschi E,Zunino R,McBride HM

doi

10.1038/embor.2009.86

subject

Has Abstract

pub_date

2009-07-01 00:00:00

pages

748-54

issue

7

eissn

1469-221X

issn

1469-3178

pii

embor200986

journal_volume

10

pub_type

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