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. Author manuscript; available in PMC: 2014 Jul 2.
Published in final edited form as: Nat Rev Mol Cell Biol. 2014 Mar;15(3):163–177. doi: 10.1038/nrm3753

Table 2.

IF protein PTMs, modifying enzymes, and methods of analysis

PTM IFs PTM enzyme (on) PTM enzyme (off) Tools for PTM analysis
Extensively studied
Phosphorylation most IFs* SAPKs, AKT1, PKC, Cdk1, Cdk5, other PP1, PP2A LC-MS; antibodies; phosphomutant transgenic mice; enzyme inhibitors
Farnesylation lamins farnesyl transferase Zmpste24 (via proteolysis) Zmpste−/− mice, FTIs
Ubiquitination most IFs** CHIP/STUB, Ubc3, UbcH5, Siah1, Trim32 not known LC-MS, in vitro ubiquitination; stress models; proteasome inhibitors
Accumulating data
Sumoylation lamins
keratins
vimentin
Ubc9 not known LC-MS; in vitro sumoylation, SUMO antibodies
Glycosylation keratins
neurofilaments
vimentin
OGT O-GlcNAcase LC-MS, transgenic mice (for example, K18-Gly-), antibodies (for example, NL6)
Acetylation keratins not known SIRT2 LC-MS, pan-acetyllysine antibodies, acid-urea gels, deacetylase inhibitors
Limited data
Transamidation keratins transglutaminases none in vitro and in vivo cross-linking analysis
ADP ribosylation desmin
vimentin
ADP-ribosyl transferase SpyA not known LC-MS, in vitro ribosylation
*

phosphorylation of filensin, phakinin, and syncoilin is based on proteomic evidence

**

putative ubiquitination sites for most IFs have been identified by large scale proteomic studies