3D Structure and Interaction of p24β and p24δ Golgi Dynamics Domains: Implication for p24 Complex Formation and Cargo Transport

Nagae, Masamichi; Hirata, Tetsuya; Morita-Matsumoto, Kana; Theiler, Romina; Fujita, Morihisa; Kinoshita, Taroh; Yamaguchi, Yoshiki

doi:10.1016/j.jmb.2016.08.023

Cited by 41 publications

(64 citation statements)

References 43 publications

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“…Two cysteine residues, Cys47 and Cys107, form a disulfide bond that bridges β2 and β7 strands. This cysteine pair is completely conserved among all p24 GOLD domains, and the disulfide bond is also seen in the corresponding sites of p24β1 and p24δ1 GOLD domains . This indicates that the disulfide bridge plays a structural role to maintain the β‐sandwich fold of p24 GOLD domains.…”

Section: Resultsmentioning

confidence: 79%

“…(C)]. In contrast, p24β1 does not dimerize and is present as a monomer in the crystal, possibly because the pairs of polar residues in the β1 strand are not fully conserved as in p24δ1 [Fig. (A)].…”

Section: Resultsmentioning

confidence: 99%

“…Our biochemical analyses suggest that a hetero‐tetrameric complex of p24α2, p24β1, p24δ1, and p24γ2 is engaged in the selective transport of glycosylphosphatidylinositol anchored proteins (GPI‐APs) in mammalian cells . To support this idea, we recently found that p24β1 interacts directly with p24δ1 through their GOLD domains …”

Section: Introductionmentioning

confidence: 80%

“…The role of p24 complex formation in cargo transport is not fully understood from the 3D structural point of view. To gain insight into the transport machinery, we recently determined crystal structures of p24δ1 and p24β1 GOLD domains and clarified the heterophilic interaction between the two GOLD domains . Comprehensive biochemical and structural analyses of p24 proteins will be necessary to reveal atomic details of the selective transport mechanism.…”

Section: Introductionmentioning

confidence: 99%

“…9,10 To support this idea, we recently found that p24b1 interacts directly with p24d1 through their GOLD domains. 11 Among p24 family members, the p24g subfamily is thought to participate in the direct recognition of each cargo protein. Amino acid sequence alignment of five p24g subfamily proteins (p24g1-p24g5) demonstrates that p24g1 is close to p24g2 (54% identity) while p24g3 and p24g4 share many amino acid residues (62% identity) [ Fig.…”

Section: Introductionmentioning

confidence: 99%

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Crystallographic analysis of murine p24γ2 Golgi dynamics domain

et al. 2017

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The p24 family proteins form homo- and hetero-oligomeric complexes for efficient transport of cargo proteins from the endoplasmic reticulum to the Golgi apparatus. It consists of four subfamilies (p24α, p24β, p24γ, and p24δ). p24γ2 plays crucial roles in the selective transport of glycosylphosphatidylinositol-anchored proteins. Here, we determined the crystal structure of mouse p24γ2 Golgi dynamics (GOLD) domain at 2.8 Å resolution by the single anomalous diffraction method using intrinsic sulfur atoms. In spite of low sequence identity among p24 family proteins, p24γ2 GOLD domain assumes a β-sandwich fold, similar to that of p24β1 or p24δ1. An additional short α-helix is observed at the C-terminus of the p24γ2 GOLD domain. Intriguingly, p24γ2 GOLD domains crystallize as dimers, and dimer formation seems assisted by the short α-helix. Dimerization modes of GOLD domains are compared among p24 family proteins. Proteins 2017; 85:764-770. © 2016 Wiley Periodicals, Inc.

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Section: Resultsmentioning

confidence: 79%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 80%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Crystallographic analysis of murine p24γ2 Golgi dynamics domain

et al. 2017

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A gold revision of the Golgi Dynamics (GOLD) domain structure and associated cell functionalities

Mendes

Costa-Filho

2022

FEBS Letters

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The classical secretory pathway is the key membrane-based delivery system in eukaryotic cells. Several families of proteins involved in the secretory pathway, with functionalities going from cargo sorting receptors to the maintenance and dynamics of secretory organelles, share soluble globular domains predicted to mediate protein-protein interactions. One of them is the 'Golgi Dynamics' (GOLD) domain, named after its strong association with the Golgi apparatus. There are many GOLD-containing protein families, such as the transmembrane emp24 domain-containing proteins (TMED/p24 family), animal SEC14-like proteins, human Golgi resident protein ACBD3, a splice variant of TICAM2 called TRAM with GOLD domain, and FYCO1. Here, we critically review the state-of-the-art knowledge of the structures and functions of the main representatives of GOLD-containing proteins in vertebrates. We provide the first unified description of the GOLD domain structure across different families since the first high-resolution structure was determined. With a brand-new update on the definition of the GOLD domain, we also discuss how its tertiary structure fits the b-sandwich-like fold map and give exciting new directions for forthcoming studies.

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Biophysical Analyses for Probing Glycan-Protein Interactions

Nagae

Yamaguchi

2018

Glycobiophysics

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Glycan-protein interactions occur at many physiological events, and the analyses are of considerable importance for understanding glycan-dependent mechanisms. Biophysical approaches including 3D structural analysis are essential for revealing glycan-protein interactions at the atomic level. The inherent diversity of glycans suits them to function as identification tags, e.g., distinguish self from the nonself components of pathogens. However, the complexity of glycans and poor affinities for interaction partners limit the usefulness of conventional analyses. To cope with such troublesome glycans, a logical sequence of biophysical analyses need to be developed. In this chapter, we introduce a workflow of glycan-protein interaction analysis consisting of six steps: preparation of lectin and glycan, screening of glycan ligand, determination of binding epitope, quantitative interaction analysis, 3D structural analysis, and molecular dynamics simulation. Our increasing knowledge and understanding of lectin-glycan interactions will hopefully lead to the design of glyco-based medicines and vaccines.

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3D Structure and Interaction of p24β and p24δ Golgi Dynamics Domains: Implication for p24 Complex Formation and Cargo Transport

Cited by 41 publications

References 43 publications

Crystallographic analysis of murine p24γ2 Golgi dynamics domain

Crystallographic analysis of murine p24γ2 Golgi dynamics domain

A gold revision of the Golgi Dynamics (GOLD) domain structure and associated cell functionalities

Biophysical Analyses for Probing Glycan-Protein Interactions

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