ArticleJournal of molecular cell biology2017
Human apo-SRP72 and SRP68/72 complex structures reveal the molecular basis of protein translocation.
Article in Journal of molecular cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
- Machine learning-based integration identifies lactylation biomarkers for prognosis prediction and tumor microenvironment modulation in bladder cancer.Translational andrology and urology · 2026Article
- A De Novo Splicing Mutation of SRP72 in Bone Marrow Failure Syndrome Type 1: Case Report and Review of the Literature.Molecular genetics & genomic medicine · 2026Review
- Exploration of the Prognostic Markers of Multiple Myeloma Based on Cuproptosis-Related Genes.Cancer reports (Hoboken, N.J.) · 2025Article
- Cryo-EM structure of SRP68/72 reveals an extended dimerization domain with RNA-binding activity.Nucleic acids research · 2024Article
- Pathogenic signal peptide variants in the human genome.NAR genomics and bioinformatics · 2023Article
- Closer to the Reality-Proteome Changes Evoked by Endometrial Scratching in Fertile Females.International journal of molecular sciences · 2023Article
- Deep genomic characterization highlights complexities and prognostic markers of pediatric acute myeloid leukemia.Communications biology · 2023Article
- Structures of MPND Reveal the Molecular Recognition of Nucleosomes.International journal of molecular sciences · 2023Article
- Structure of Rift Valley Fever Virus RNA-Dependent RNA Polymerase.Journal of virology · 2022Article
- Structural Basis of Human Parainfluenza Virus 3 Unassembled Nucleoprotein in Complex with Its Viral Chaperone.Journal of virology · 2022Article
- Signal Recognition Particle in Human Diseases.Frontiers in genetics · 2022Article
- Proteomic-Based Machine Learning Analysis Reveals PYGB as a Novel Immunohistochemical Biomarker to Distinguish Inverted Urothelial Papilloma From Low-Grade Papillary Urothelial Carcinoma With Inverted Growth.Frontiers in oncology · 2022Article
- SRPassing Co-translational Targeting: The Role of the Signal Recognition Particle in Protein Targeting and mRNA Protection.International journal of molecular sciences · 2021Review
- Identification of biallelic germline variants of SRP68 in a sporadic case with severe congenital neutropenia.Haematologica · 2021Article
- Crystal structures of REF6 and its complex with DNA reveal diverse recognition mechanisms.Cell discovery · 2020Article
- Hydrophobicity, rather than secondary structure, is essential for the SRP dependent targeting of GPR35 to the ER membrane.Journal of bioenergetics and biomembranes · 2019Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The co-translational targeting or insertion of secretory and membrane proteins into the endoplasmic reticulum (ER) is a key biological process mediated by the signal recognition particle (SRP). In eukaryotes, the SRP68-SRP72 (SRP68/72) heterodimer plays an essential role in protein translocation. However, structural information on the two largest SRP proteins, SRP68 and SRP72, is limited, especially regarding their interaction. Herein, we report the first crystal structures of human apo-SRP72 and the SRP68/72 complex at 2.91Å and 1.7Å resolution, respectively. The SRP68-binding domain of SRP72 contains four atypical tetratricopeptide repeats (TPR) and a flexible C-terminal cap. Apo-SRP72 exists mainly as dimers in solution. To bind to SRP68, the SRP72 homodimer disassociates, and the indispensable C-terminal cap undergoes a pronounced conformational change to assist formation of the SRP68/72 heterodimer. A 23-residue polypeptide of SRP68 is sufficient for tight binding to SRP72 through its unusually hydrophobic and extended surface. Structural, biophysical, and mutagenesis analyses revealed that cancer-associated mutations disrupt the SRP68-SRP72 interaction and their co-localization with ER in mammalian cells. The results highlight the essential role of the SRP68-SRP72 interaction in SRP-mediated protein translocation and provide a structural basis for disease diagnosis, pathophysiology, and drug design.
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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.