ArticleInternational journal of molecular sciences2015
Structural analysis of the complex between penta-EF-hand ALG-2 protein and Sec31A peptide reveals a novel target recognition mechanism of ALG-2.
Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 35 citations in OpenAlex.
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- Annexin, a Protein for All Seasons: From Calcium Dependent Membrane Metabolism to RNA Recognition.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Mechanism and cellular function of direct membrane binding by the ESCRT and ERES-associated CaProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mechanism and cellular function of direct membrane binding by the ESCRT and ERES-associated CabioRxiv : the preprint server for biology · 2023Article
- Biallelic NovelMolecular syndromology · 2023Article
- Tibolone Pre-Treatment Ameliorates the Dysregulation of Protein Translation and Transport Generated by Palmitic Acid-Induced Lipotoxicity in Human Astrocytes: A Label-Free MS-Based Proteomics and Network Analysis.International journal of molecular sciences · 2022Article
- The Novel ALG-2 Target Protein CDIP1 Promotes Cell Death by Interacting with ESCRT-I and VAPA/B.International journal of molecular sciences · 2021Article
- The Penta-EF-Hand ALG-2 Protein Interacts with the Cytosolic Domain of the SOCE Regulator SARAF and Interferes with Ubiquitination.International journal of molecular sciences · 2020Article
- Verification of theInternational journal of molecular sciences · 2019Article
- Thermodynamic Characterization of the CaInternational journal of molecular sciences · 2018Article
- Flexibility of the Sec13/31 cage is influenced by the Sec31 C-terminal disordered domain.Journal of structural biology · 2018Article
- Nanoluciferase Reporter Gene System Directed by Tandemly Repeated Pseudo-Palindromic NFAT-Response Elements Facilitates Analysis of Biological Endpoint Effects of Cellular CaInternational journal of molecular sciences · 2018Article
- ALG-2 participates in recovery of cells after plasma membrane damage by electroporation and digitonin treatment.PloS one · 2018Article
- The calcium-binding protein ALG-2 regulates protein secretion and trafficking via interactions with MISSL and MAP1B proteins.The Journal of biological chemistry · 2017Article
- Structural and Functional Study of Apoptosis-linked Gene-2·Heme-binding Protein 2 Interactions in HIV-1 Production.The Journal of biological chemistry · 2016Article
- TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Multifaceted Roles of ALG-2 in Ca(2+)-Regulated Membrane Trafficking.International journal of molecular sciences · 2016Review
- Structural basis of Sorcin-mediated calcium-dependent signal transduction.Scientific reports · 2015Article
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Authors and funding
11 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ALG-2, a 22-kDa penta-EF-hand protein, is involved in cell death, signal transduction, membrane trafficking, etc., by interacting with various proteins in mammalian cells in a Ca2+-dependent manner. Most known ALG-2-interacting proteins contain proline-rich regions in which either PPYPXnYP (type 1 motif) or PXPGF (type 2 motif) is commonly found. Previous X-ray crystal structural analysis of the complex between ALG-2 and an ALIX peptide revealed that the peptide binds to the two hydrophobic pockets. In the present study, we resolved the crystal structure of the complex between ALG-2 and a peptide of Sec31A (outer shell component of coat complex II, COPII; containing the type 2 motif) and found that the peptide binds to the third hydrophobic pocket (Pocket 3). While amino acid substitution of Phe85, a Pocket 3 residue, with Ala abrogated the interaction with Sec31A, it did not affect the interaction with ALIX. On the other hand, amino acid substitution of Tyr180, a Pocket 1 residue, with Ala caused loss of binding to ALIX, but maintained binding to Sec31A. We conclude that ALG-2 recognizes two types of motifs at different hydrophobic surfaces. Furthermore, based on the results of serial mutational analysis of the ALG-2-binding sites in Sec31A, the type 2 motif was newly defined.
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