ArticleScientific reports2016
Dissecting the structural basis of MEIG1 interaction with PACRG.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Male infertility.Systems biology in reproductive medicine · 2025Review
- In Silico Discovery of Potential Inhibitors Targeting the MEIG1-PACRG Complex for Male Contraceptive Development.Proteins · 2025Article
- Function of manchette and intra-manchette transport in spermatogenesis and male fertility.Cell communication and signaling : CCS · 2025Review
- Article
- Article
- Single-Cell RNA Sequencing of the Testis ofCells · 2022Article
- Marginal Zinc Deficiency in Mice Increased the Number of Abnormal Sperm and Altered the Expression Level of Spermatogenesis-Related Genes.Biological trace element research · 2022Article
- Identification and functional analysis ofFrontiers in physiology · 2022Article
- Crystal structure of human PACRG in complex with MEIG1 reveals roles in axoneme formation and tubulin binding.Structure (London, England : 1993) · 2021Article
- Functional Expression, Purification and Identification of Interaction Partners of PACRG.Molecules (Basel, Switzerland) · 2021Article
- Intraflagellar transport protein IFT20 is essential for male fertility and spermiogenesis in mice.Molecular biology of the cell · 2016Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
The product of the meiosis-expressed gene 1 (MEIG1) is found in the cell bodies of spermatocytes and recruited to the manchette, a structure unique to elongating spermatids, by Parkin co-regulated gene (PACRG). This complex is essential for targeting cargo to the manchette during sperm flagellum assembly. Here we show that MEIG1 adopts a unique fold that provides a large surface for interacting with other proteins. We mutated 12 exposed and conserved amino acids and show that four of these mutations (W50A, K57E, F66A, Y68A) dramatically reduce binding to PACRG. These four amino acids form a contiguous hydrophobic patch on one end of the protein. Furthermore, each of these four mutations diminishes the ability of MEIG1 to stabilize PACRG when expressed in bacteria. Together these studies establish the unique structure and key interaction surface of MEIG1 and provide a framework to explore how MEIG1 recruits proteins to build the sperm tail.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.