Protein acyl thioesterases (Review)

Zeidman, Ruth; Jackson, Caroline S.; Magee, Anthony I.

doi:10.1080/09687680802629329

Cited by 112 publications

(104 citation statements)

References 90 publications

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“…Kinetic Characterization of FTT258 and hAPT1-Acyl protein thioesterases are a highly conserved subclass of serine hydrolases with diverse intracellular substrates and significant therapeutic applications (16). Based on the role of bacterial lipoproteins in the virulence of F. tularensis and the confirmed pharmacological importance of hAPT1 (18), we sought to identify and study an APT1 homologue from F. tularensis and compare it to hAPT1.…”

Section: Resultsmentioning

confidence: 99%

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Large Scale Structural Rearrangement of a Serine Hydrolase from Francisella tularensis Facilitates Catalysis

Filippova

Weston

Kuhn

et al. 2013

Journal of Biological Chemistry

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Background: Acyl protein thioesterases control protein S-acylation at cellular membranes. Results: FTT258 is a serine hydrolase with broad substrate specificity that binds to bacterial membranes and exists in two distinct conformations. Conclusion: Conformational changes in FTT258 are correlated with catalytic activity. Significance: Structural rearrangement dually regulates the membrane binding and catalytic activity of acyl protein thioesterases.

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Section: Resultsmentioning

confidence: 99%

“…A conserved conformational change for hAPT1 would link the biological role of hAPT1 in recycling proteins such as Ras from the plasma membrane with the cellular location for this role (16). hAPT1 has a conserved tryptophan and a conservatively substituted phenylalanine for tyrosine in its ␤ 3 loop (Table 2).…”

Section: Discussionmentioning

confidence: 99%

Large Scale Structural Rearrangement of a Serine Hydrolase from Francisella tularensis Facilitates Catalysis

Filippova

Weston

Kuhn

et al. 2013

Journal of Biological Chemistry

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“…Two of these thioesterases, acyl-protein thioesterase-1 (APT1) (11) and APT2 (12), are localized predominantly in the cytoplasm, and the other two, palmitoyl-protein thioesterase-1 (PPT1) (13,14) and PPT2 (15), are lysosomal enzymes (16,17). The first cytosolic thioesterase to be characterized was APT1, which cat-alyzed depalmitoylation of the ␣-subunit of G-proteins and proto-oncogene H-Ras product in vitro (11) as well as synaptosomal-associated protein 23 (SNAP-23) (18). More recently, a second cytosolic thioesterase, APT2, has been reported to depalmitoylate GAP-43 (growth-associated protein 43) (12).…”

mentioning

confidence: 99%

Dynamic Palmitoylation Links Cytosol-Membrane Shuttling of Acyl-protein Thioesterase-1 and Acyl-protein Thioesterase-2 with That of Proto-oncogene H-Ras Product and Growth-associated Protein-43

Kong

Peng

Chandra

et al. 2013

Journal of Biological Chemistry

123

145

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Background: How cytosolic thioesterases (APT1 and APT2) depalmitoylate their membrane-anchored substrates remains unclear. Results: APT1 and APT2 require palmitoylation for membrane localization. Although APT1 depalmitoylates itself, H-Ras, and APT2, APT2 depalmitoylates GAP-43. Conclusion: Dynamic palmitoylation regulates steady-state membrane localization and function of cytosolic thioesterases and their substrates. Significance: The findings may provide new insight into the regulation and function of cytosolic thioesterases and their substrates.

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“…Palmitoylation is not only found in combination with other types of acylation; some proteins can also be uniquely modified by palmitoylation, however the molecular basis that mediates the initial contact with the membrane remains to be identified. Given that palmitoylation is reversible, a depalmitoylation reaction can occur and is catalysed by a class of enzymes known as acyl protein thioesterases (APTs) or palmitoyl protein thioesterases (PPTs) (Camp and Hofmann, 1993;Zeidman et al, 2009). It is conceivable that palmitoylation/depalmitoylation cycles constitute an efficient way to modulate the functions of proteins and biological processes.…”

Section: Acylation Impacts On the Fate Of Proteinsmentioning

confidence: 99%

Emerging roles for protein S-palmitoylation in Toxoplasma biology

Frénal

Kemp

Soldati‐Favre

2014

International Journal for Parasitology

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a b s t r a c tPost-translational modifications are refined, rapidly responsive and powerful ways to modulate protein function. Among post-translational modifications, acylation is now emerging as a widespread modification exploited by eukaryotes, bacteria and viruses to control biological processes. Protein palmitoylation involves the attachment of palmitic acid, also known as hexadecanoic acid, to cysteine residues of integral and peripheral membrane proteins and increases their affinity for membranes. Importantly, similar to phosphorylation, palmitoylation is reversible and is becoming recognised as instrumental for the regulation of protein function by modulating protein interactions, stability, folding, trafficking and signalling. Palmitoylation appears to play a central role in the biology of the Apicomplexa, regulating critical processes such as host cell invasion which is vital for parasite survival and dissemination. The recent identification of over 400 palmitoylated proteins in Plasmodium falciparum erythrocytic stages illustrates the broad spread and impact of this modification on parasite biology. The main enzymes responsible for protein palmitoylation are multi-membrane protein S-acyl transferases harbouring a catalytic Asp-HisHis-Cys (DHHC) motif. A global functional analysis of the repertoire of protein S-acyl transferases in Toxoplasma gondii and Plasmodium berghei has recently been performed. The essential nature of some of these enzymes illustrates the key roles played by this post-translational modification in the corresponding substrates implicated in fundamental processes such as parasite motility and organelle biogenesis. Toward a better understanding of the depalmitoylation event, a protein with palmitoyl protein thioesterase activity has been identified in T. gondii. TgPPT1/TgASH1 is the main target of specific acyl protein thioesterase inhibitors but is dispensable for parasite survival, suggesting the implication of other genes in depalmitoylation. Palmitoylation/depalmitoylation cycles are now emerging as potential novel regulatory networks and T. gondii represents a superb model organism in which to explore their significance.

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Protein acyl thioesterases (Review)

Cited by 112 publications

References 90 publications

Large Scale Structural Rearrangement of a Serine Hydrolase from Francisella tularensis Facilitates Catalysis

Large Scale Structural Rearrangement of a Serine Hydrolase from Francisella tularensis Facilitates Catalysis

Dynamic Palmitoylation Links Cytosol-Membrane Shuttling of Acyl-protein Thioesterase-1 and Acyl-protein Thioesterase-2 with That of Proto-oncogene H-Ras Product and Growth-associated Protein-43

Emerging roles for protein S-palmitoylation in Toxoplasma biology

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