2008
DOI: 10.1016/j.febslet.2008.02.079
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TTLL10 is a protein polyglycylase that can modify nucleosome assembly protein 1

Abstract: Certain proteins can undergo polyglycylation and polyglutamylation. Polyglutamylases (glutamate ligases) have recently been identified in a family of tubulin tyrosine ligase-like (TTLL) proteins. However, no polyglycylase (glycine ligase) has yet been reported. Here we identify a polyglycylase in the TTLL proteins by using an anti-poly-glycine antibody. The antibody reacted with a cytoplasmic 60-kDa protein that accumulated in elongating spermatids. Using tandem mass spectrometry of trypsinized samples, immuno… Show more

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Cited by 45 publications
(43 citation statements)
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“…In D. melanogaster, DmTTLL3A mono-and polyglycylates the ␣-and the ␤-tubulin, whereas DmTTLL3B mono-and polyglycylates non-tubulin proteins (10). Notably, mammalian TTLL10 is also able to act as a bifunctional enzyme on nucleosome assembly proteins (8). The evidence that gTTLL3 is the only member of the giardial TTLL family clustering close to other mono-and polyglycylases and that G. duodenalis does not have a TTLL10 homolog protein (Ref.…”
Section: Discussionmentioning
confidence: 94%
See 1 more Smart Citation
“…In D. melanogaster, DmTTLL3A mono-and polyglycylates the ␣-and the ␤-tubulin, whereas DmTTLL3B mono-and polyglycylates non-tubulin proteins (10). Notably, mammalian TTLL10 is also able to act as a bifunctional enzyme on nucleosome assembly proteins (8). The evidence that gTTLL3 is the only member of the giardial TTLL family clustering close to other mono-and polyglycylases and that G. duodenalis does not have a TTLL10 homolog protein (Ref.…”
Section: Discussionmentioning
confidence: 94%
“…Deglycylation of nuclear proteins, such as transcriptional or chromatin remodeling factors, might be responsible for the defect in encystation most clearly observed in the FLAG-gDIP2 transgenic line. It has been proposed that glycylation by TTLL10 of nucleosome assembly protein 1 (NAP1) in the mouse might modulate NAP1-histone interactions, thus inducing transcriptional repression during spermiogenesis (8). In D. melanogaster, depletion of DmTTLL3B protein results in several defects attributed to the potential lack of glycylation of its substrates, including chaperonins and motor proteins (10).…”
Section: Discussionmentioning
confidence: 99%
“…This simple addition of a mere polypeptide that has no outstanding characteristic had made it difficult for researchers to anticipate the function of the modification. However, the roles of tubulin polyglycylation are now beginning to be unveiled, as TTLLs 3, 8, and 10 are identified as polyglycylation-performing enzymes, the polyglycylases (or glycine ligases) (Ikegami et al, 2008;Ikegami and Setou, 2009;Rogowski et al, 2009;Wloga et al, 2009b).…”
Section: Polyglycylationmentioning
confidence: 99%
“…41 Mutation of Pgs1 (GTRGEO22) in ROSA22 mice has been associated with male sterility and neuronal defects. 7 Subsequent analysis of the these Pgs1-mutant mice has revealed a notable loss of polyglutamylation on a tubulin, 25 indicating that PGs1 is important for tubulin polyglutamylation. PGs1 lacks catalytic activity, but its localization at tubulin polyglutamylation sites in neurons, axonemes, and centrioles 46 suggests that it, like the fleer protein in zebrafish, may be involved in the regulation, localization, or transport of the larger polyglutamylase complex.…”
Section: Discussionmentioning
confidence: 99%