2011
DOI: 10.1371/journal.pbio.1001073
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N-Terminal Acetylation Inhibits Protein Targeting to the Endoplasmic Reticulum

Abstract: Amino-terminal acetylation is probably the most common protein modification in eukaryotes with as many as 50%–80% of proteins reportedly altered in this way. Here we report a systematic analysis of the predicted N-terminal processing of cytosolic proteins versus those destined to be sorted to the secretory pathway. While cytosolic proteins were profoundly biased in favour of processing, we found an equal and opposite bias against such modification for secretory proteins. Mutations in secretory signal sequences… Show more

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Cited by 177 publications
(174 citation statements)
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“…For some proteins, N-terminal acetylation may act as a degradation signal (88), whereas for others N-terminal acetylation may protect from proteolytic degradation and subsequently increases their half-life (89). N-terminal acetylation was also shown to be involved in protein sorting and addressing to cellular organelles (90) or to membrane (91). Indeed, although Adh1p is frequently described as a cytoplasmic protein, it is also associated with the plasma membrane (92) like many other fermentation enzymes (Pgi1p, Tpi1p, Eno1p, Eno2p, Tdh1p, Tdh2p, Tdh3p, Pgk1p, Pyk1p).…”
Section: Discussionmentioning
confidence: 99%
“…For some proteins, N-terminal acetylation may act as a degradation signal (88), whereas for others N-terminal acetylation may protect from proteolytic degradation and subsequently increases their half-life (89). N-terminal acetylation was also shown to be involved in protein sorting and addressing to cellular organelles (90) or to membrane (91). Indeed, although Adh1p is frequently described as a cytoplasmic protein, it is also associated with the plasma membrane (92) like many other fermentation enzymes (Pgi1p, Tpi1p, Eno1p, Eno2p, Tdh1p, Tdh2p, Tdh3p, Pgk1p, Pyk1p).…”
Section: Discussionmentioning
confidence: 99%
“…However, an increasing number of reports indicate that Nt-acetylation is essential for higher eukaryotes, but less critical for normal growth in yeast (9)(10)(11)(12). Functionally, Nt-acetylation was found to regulate a variety of protein features (13), including the degradation (at least in yeast) of some Nt-acetylated proteins by a new branch of the Nend-rule pathway (14) and the ability of Nt-acetylation to inhibit protein translocation into the endoplasmic reticulum (15). The major NATs, NatA, -B, and -C are heterodimers or heterotrimers.…”
mentioning
confidence: 99%
“…Most recently two studies have significantly revisited the field of acetylation function and regulation. First, it was suggested that NAA contributes to cell sorting by inhibiting protein to target the endoplasmic reticulum (39). Thus, proteins devoid of NAA signal would be preferentially guided to the secretory pathway in yeast.…”
mentioning
confidence: 99%