Interaction of Leishmania PTS2 receptor peroxin 7 with the glycosomal protein import machinery

Pilar, Ana Victoria C.; Madrid, Kleber P.; Jardim, Armando

doi:10.1016/j.molbiopara.2007.11.013

Cited by 26 publications

(34 citation statements)

References 48 publications

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“…9B). The differential centrifugation protocol that was employed has been shown previously to yield intact glycosomes (65,66). Further fractionation of the post-nuclear cell lysates on a sucrose gradient revealed that PEX14, a known glycosomal marker, cosedimented with the glycosomes (lower portion of the gradient, fractions 15-28) (57), whereas ASL could be detected exclusively at the top of the sucrose gradient (fractions 1-14) with other cytosolic enzymes (Fig.…”

Section: Resultsmentioning

confidence: 92%

Adenylosuccinate Synthetase and Adenylosuccinate Lyase Deficiencies Trigger Growth and Infectivity Deficits in Leishmania donovani

Boitz

Strasser

Yates

et al. 2013

Journal of Biological Chemistry

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Section: Resultsmentioning

confidence: 92%

Adenylosuccinate Synthetase and Adenylosuccinate Lyase Deficiencies Trigger Growth and Infectivity Deficits in Leishmania donovani

Boitz

Strasser

Yates

et al. 2013

Journal of Biological Chemistry

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“…4A). The differential centrifugation protocol that was employed has been shown previously to yield intact glycosomes (80,81). The AAH co-sedimented with APRT, a cytosolic marker (13), whereas IMPDH, a known glycosomal enzyme (57), was associated exclusively with the organellar (45,000 ϫ g) pellet (Fig.…”

Section: Multiple Sequence Alignment Of L Donovani Aah-the Lmentioning

confidence: 90%

Adenine Aminohydrolase from Leishmania donovani

Boitz

Strasser

Hartman

et al. 2012

Journal of Biological Chemistry

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Background: Purine salvage in Leishmania is an indispensable nutritional process. Results: Adenine aminohydrolase, a key purine enzyme in Leishmania, has been characterized biochemically and genetically. Conclusion: Adenine aminohydrolase is a unique enzyme in purine salvage that converts 6-aminopurines into 6-oxypurines. Significance: Functional characterization of key enzymes is crucial for understanding purine salvage and ultimately for targeting the pathway with drugs.

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“…Rather less is known about Pex7p than Pex5p, as attempts to express and purify this protein have been met with limited success (Mukai and Fujiki, 2006;Pilar et al, 2008). Unlike Pex5p, Pex7p does not act autonomously, but requires the action of auxiliary proteins as co-receptors, as detailed in the following section.…”

Section: Pex7p Receptormentioning

confidence: 99%

Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes

Lanyon‐Hogg

Warriner

Baker

2010

Biology of the Cell

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Peroxisomes are a family of organelles which have many unusual features. They can arise de novo from the endoplasmic reticulum by a still poorly characterized process, yet possess a unique machinery for the import of their matrix proteins. As peroxisomes lack DNA, their function, which is highly variable and dependent on developmental and/or environmental conditions, is determined by the post-translational import of specific metabolic enzymes in folded or oligomeric states. The two classes of matrix targeting signals for peroxisomal proteins [PTS1 (peroxisomal targeting signal 1) and PTS2] are recognized by cytosolic receptors [PEX5 (peroxin 5) and PEX7 respectively] which escort their cargo proteins to, or possibly across, the peroxisome membrane. Although the membrane translocation mechanism remains unclear, it appears to be driven by thermodynamically favourable binding interactions. Recycling of the receptors from the peroxisome membrane requires ATP hydrolysis for two linked processes: ubiquitination of PEX5 (and the PEX7 co-receptors in yeast) and the function of two peroxisome-associated AAA (ATPase associated with various cellular activities) ATPases, which play a role in recycling or turnover of the ubiquitinated receptors. This review summarizes and integrates recent findings on peroxisome matrix protein import from yeast, plant and mammalian model systems, and discusses some of the gaps in our understanding of this remarkable protein transport system.

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Interaction of Leishmania PTS2 receptor peroxin 7 with the glycosomal protein import machinery

Cited by 26 publications

References 48 publications

Adenylosuccinate Synthetase and Adenylosuccinate Lyase Deficiencies Trigger Growth and Infectivity Deficits in Leishmania donovani

Adenylosuccinate Synthetase and Adenylosuccinate Lyase Deficiencies Trigger Growth and Infectivity Deficits in Leishmania donovani

Adenine Aminohydrolase from Leishmania donovani

Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes

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