Comparative Genomics and Adaptive Selection of the ATP-Binding-Cassette Gene Family in Caenorhabditis Species

Zhao, Zhongying; Thomas, James H.; Chen, Nansheng; Sheps, Jonathan A.; Baillie, David L.

doi:10.1534/genetics.106.066720

Cited by 26 publications

(36 citation statements)

References 50 publications

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“…In mammals, antigenic peptides are translocated from the cytosol into the ER via the transporter associated with antigen processing (TAP), a member of the ATP binding cassette (ABC) transporter family. Although C. elegans, like other invertebrates, do not possess MHC molecules or other components of an adaptive immune system, they do possess 60 members of the ABC transporter family, including several TAPlike genes (Zhao et al, 2007), suggesting the possibility that a cytosolic peptide or proteolytic fragment may reenter the ER and be processed through the secretory pathway (Fig. 9), although such a pathway has not been demonstrated.…”

Section: Discussionmentioning

confidence: 99%

TheN-Glycanasepng-1Acts to Limit Axon Branching during Organ Formation in Caenorhabditis elegans

Habibi-Babadi

Su²,

Carvalho³

et al. 2010

J. Neurosci.

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Peptide:N-glycanases (PNGases) are cytoplasmic de-N-glycosylation enzymes that have been shown in cultured cells to facilitate the degradation of misfolded glycoproteins during endoplasmic reticulum-associated degradation and in the processing of major histocompatibility complex class I antigens for proper cell-surface presentation. The gene encoding PNGase activity was initially described in budding yeast (Png1p) and shown to be highly conserved from yeast to humans, but physiological roles in higher organisms have not been elucidated. Here we describe peripheral nervous system defects associated with the first loss-of-function mutations in an animal PNGase. Mutations in png-1, the Caenorhabditis elegans PNGase ortholog, result in an increase in axon branching during morphogenesis of the vulval egg-laying organ and egg-laying behavior changes. Neuronal defects include an increase in the branched morphology of the VC4 and VC5 egg-laying neurons as well as inappropriate branches from axons that run adjacent to the vulva but would normally remain unbranched. We show that png-1 is widely expressed and can act from both neurons and epithelial cells to restrict axon branching. A deletion allele of the DNA repair gene rad-23, orthologs of which are known to physically interact with PNGases in yeast and mammals, displays similar axon branching defects and genetic interactions with png-1. In summary, our analysis reveals a novel developmental role for a PNGase and Rad-23 in the regulation of neuronal branching during organ innervation.

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Section: Discussionmentioning

confidence: 99%

TheN-Glycanasepng-1Acts to Limit Axon Branching during Organ Formation in Caenorhabditis elegans

Habibi-Babadi

Su²,

Carvalho³

et al. 2010

J. Neurosci.

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“…2 and see Fig. 4); these ABC proteins do not function as transporters but instead are likely to couple ATP hydrolysis to other processes such as DNA repair and protein translation (78,174,175).…”

Section: Nucleotide-binding Domains Are the Diagnostic Features Of Abmentioning

confidence: 99%

ABC Transporters in Saccharomyces cerevisiae and Their Interactors: New Technology Advances the Biology of the ABCC (MRP) Subfamily

Paumi¹,

Chuk

Snider

et al. 2009

Microbiol Mol Biol Rev

165

175

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SUMMARY Members of the ATP-binding cassette (ABC) transporter superfamily exist in bacteria, fungi, plants, and animals and play key roles in the efflux of xenobiotic compounds, physiological substrates, and toxic intracellular metabolites. Based on sequence relatedness, mammalian ABC proteins have been divided into seven subfamilies, ABC subfamily A (ABCA) to ABCG. This review focuses on recent advances in our understanding of ABC transporters in the model organism Saccharomyces cerevisiae. We propose a revised unified nomenclature for the six yeast ABC subfamilies to reflect the current mammalian designations ABCA to ABCG. In addition, we specifically review the well-studied yeast ABCC subfamily (formerly designated the MRP/CFTR subfamily), which includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p). We focus on Ycf1p, the best-characterized yeast ABCC transporter. Ycf1p is located in the vacuolar membrane in yeast and functions in a manner analogous to that of the human multidrug resistance-related protein (MRP1, also called ABCC1), mediating the transport of glutathione-conjugated toxic compounds. We review what is known about Ycf1p substrates, trafficking, processing, posttranslational modifications, regulation, and interactors. Finally, we discuss a powerful new yeast two-hybrid technology called integrated membrane yeast two-hybrid (iMYTH) technology, which was designed to identify interactors of membrane proteins. iMYTH technology has successfully identified novel interactors of Ycf1p and promises to be an invaluable tool in future efforts to comprehensively define the yeast ABC interactome.

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“…The C. elegans genome encodes 61 ABC transporters with representatives in all eight subfamilies identified in Drosophila and humans Zhao et al 2007). Functions for 18 C. elegans ABC transporters have been defined through genetic studies.…”

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confidence: 99%

Role of the Caenorhabditis elegans Multidrug Resistance Gene, mrp-4, in Gut Granule Differentiation

Currie

King

Lawrenson³

et al. 2007

Genetics

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Caenorhabditis elegans gut granules are lysosome-related organelles with birefringent contents. mrp-4, which encodes an ATP-binding cassette (ABC) transporter homologous to mammalian multidrug resistance proteins, functions in the formation of gut granule birefringence. mrp-4(À) embryos show a delayed appearance of birefringent material in the gut granule but otherwise appear to form gut granules properly. mrp-4(1) activity is required for the extracellular mislocalization of birefringent material, bodylength retraction, and NaCl sensitivity, phenotypes associated with defective gut granule biogenesis exhibited by embryos lacking the activity of GLO-1/Rab38, a putative GLO-1 guanine nucleotide exchange factor GLO-4, and the AP-3 complex. Multidrug resistance protein (MRP)-4 localizes to the gut granule membrane, consistent with it playing a direct role in the transport of molecules that compose and/or facilitate the formation of birefringent crystals within the gut granule. However, MRP-4 is also present in oocytes and early embryos, and our genetic analyses indicate that its site of action in the formation of birefringent material may not be limited to just the gut granule in embryos. In a search for genes that function similarly to mrp-4(1), we identified WHT-2, another ABC transporter that acts in parallel to MRP-4 for the formation of birefringent material in the gut granule.

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Comparative Genomics and Adaptive Selection of the ATP-Binding-Cassette Gene Family in Caenorhabditis Species

Cited by 26 publications

References 50 publications

TheN-Glycanasepng-1Acts to Limit Axon Branching during Organ Formation in Caenorhabditis elegans

TheN-Glycanasepng-1Acts to Limit Axon Branching during Organ Formation in Caenorhabditis elegans

ABC Transporters in Saccharomyces cerevisiae and Their Interactors: New Technology Advances the Biology of the ABCC (MRP) Subfamily

Role of the Caenorhabditis elegans Multidrug Resistance Gene, mrp-4, in Gut Granule Differentiation

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