ArticleCell cycle (Georgetown, Tex.)2018
Function of a membrane-embedded domain evolutionarily multiplied in the GPI lipid anchor pathway proteins PIG-B, PIG-M, PIG-U, PIG-W, PIG-V, and PIG-Z.
Article in Cell cycle (Georgetown, Tex.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 21 citations in OpenAlex.
- Genomic regions associated with bovine respiratory disease in pacific northwest Holstein cattle.Frontiers in veterinary science · 2025Article
- Molecular insights into biogenesis of glycosylphosphatidylinositol anchor proteins.Nature communications · 2022Article
- Functional Analysis of the GPI Transamidase Complex by Screening for Amino Acid Mutations in Each Subunit.Molecules (Basel, Switzerland) · 2021Article
- Hrd1-dependent Degradation of the Unassembled PIGK Subunit of the GPI Transamidase Complex.Cell structure and function · 2021Article
- Conserved sequence motifs in human TMTC1, TMTC2, TMTC3, and TMTC4, new O-mannosyltransferases from the GT-C/PMT clan, are rationalized as ligand binding sites.Biology direct · 2021Article
- Functional Classification of Super-Large Families of Enzymes Based on Substrate Binding Pocket Residues for Biocatalysis and Enzyme Engineering Applications.Frontiers in bioengineering and biotechnology · 2021Article
- Article
- Biosynthesis and biology of mammalian GPI-anchored proteins.Open biology · 2020Review
- Mutations in PIGU Impair the Function of the GPI Transamidase Complex, Causing Severe Intellectual Disability, Epilepsy, and Brain Anomalies.American journal of human genetics · 2019Article
- Article
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4 authors at 1 institution in 1 country.
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Abstract
Distant homology relationships among proteins with many transmembrane regions (TMs) are difficult to detect as they are clouded by the TMs' hydrophobic compositional bias and mutational divergence in connecting loops. In the case of several GPI lipid anchor biosynthesis pathway components, the hidden evolutionary signal can be revealed with dissectHMMER, a sequence similarity search tool focusing on fold-critical, high complexity sequence segments. We find that a sequence module with 10 TMs in PIG-W, described as acyl transferase, is homologous to PIG-U, a transamidase subunit without characterized molecular function, and to mannosyltransferases PIG-B, PIG-M, PIG-V and PIG-Z. We conclude that this new, membrane-embedded domain named BindGPILA functions as the unit for recognizing, binding and stabilizing the GPI lipid anchor in a modification-competent form as this appears the only functional aspect shared among all proteins. Thus, PIG-U's likely molecular function is shuttling/presenting the anchor in a productive conformation to the transamidase complex.
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