Curated Information
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Curated Information Page
PubMed Id: 22748923 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Leboucher GP, et al. (2012) Stress-induced phosphorylation and proteasomal degradation of mitofusin 2 facilitates mitochondrial fragmentation and apoptosis. Mol Cell 47, 547-57 22748923
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S27-p - MFN2 (human)
Orthologous residues
MFN2 (human): S27‑p, MFN2 (mouse): S27‑p, MFN2 (rat): S27‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  bone cancer
 Relevant cell lines - cell types - tissues:  HeLa (cervical), U2OS (bone cell)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE JNK2 iso2 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE JNK2 iso2 (human) siRNA inhibition of enzyme, transfection of constitutively active enzyme, co-immunoprecipitation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
doxorubicin increase
Downstream Regulation
 Effect of modification (function):  protein degradation, ubiquitination
 Effect of modification (process):  apoptosis, induced
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
HUWE1 (human) Induces co-immunoprecipitation
 Comments:  HUWE1 associates with Mfn2, and leads to Its ubiquitination and degradation.


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