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Polyglycylation

From Wikipedia, the free encyclopedia

Polyglycylation is a form of posttranslational modification of glutamate residues of the carboxyl-terminal region tubulin in certain microtubules (e.g., axonemal) originally discovered in Paramecium ,[1] and later shown in mammalian neurons as well.[2]

See also

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References

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  1. ^ Redeker V, Levilliers N, Schmitter JM, Le Caer JP, Rossier J, Adoutte A, Bré MH (1994). "Polyglycylation of tubulin: a posttranslational modification in axonemal microtubules". Science. 266 (5191): 1688–1691. Bibcode:1994Sci...266.1688R. doi:10.1126/science.7992051. PMID 7992051.
  2. ^ Banerjee Asok (2002). "Coordination of posttranslational modifications of bovine brain alpha-tubulin. Polyglycylation of delta2 tubulin". J. Biol. Chem. 277 (48): 46140–46144. doi:10.1074/jbc.M208065200 . PMID 12356754.
General
N terminus
C terminus
Single specific AAs
Serine/Threonine
Tyrosine
Cysteine
Aspartate
Glutamate
Asparagine
Glutamine
Lysine
Arginine
Proline
Histidine
Tryptophan
Crosslinks between two AAs
CysteineCysteine
MethionineHydroxylysine
LysineTyrosine
TryptophanTryptophan
Crosslinks between three AAs
SerineTyrosineGlycine
HistidineTyrosineGlycine
AlanineSerineGlycine
Crosslinks between four AAs
AllysineAllysineAllysineLysine

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