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ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

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Τίτλος: ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.
Συγγραφείς: Scott MK; School of Molecular Life Sciences, University of Victoria, Victoria, British Columbia, Canada., Klynsoon GCT; School of Molecular Life Sciences, University of Victoria, Victoria, British Columbia, Canada., Walsh EE; School of Molecular Life Sciences, University of Victoria, Victoria, British Columbia, Canada., Suresh S; School of Molecular Life Sciences, University of Victoria, Victoria, British Columbia, Canada., Nyvall HG; Department of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, British Columbia, Canada., Burke JE; School of Molecular Life Sciences, University of Victoria, Victoria, British Columbia, Canada; Department of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, British Columbia, Canada; University of Victoria Genome BC Proteomics Centre, Victoria, British Columbia, Canada. Electronic address: jeburke@uvic.ca.
Πηγή: The Journal of biological chemistry [J Biol Chem] 2026 Aug; Vol. 302 (8), pp. 113307. Date of Electronic Publication: 2026 Jun 29.
Τύπος έκδοσης: Journal Article; Research Support, Non-U.S. Gov't
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
Imprint Name(s): Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
Ιατρικοί όροι (MeSH): Guanine Nucleotide Exchange Factors*/metabolism , Guanine Nucleotide Exchange Factors*/chemistry , Golgi Apparatus*/metabolism , trans-Golgi Network*/metabolism , ADP-Ribosylation Factors*/metabolism , ADP-Ribosylation Factors*/chemistry , Phosphotransferases (Alcohol Group Acceptor)*/metabolism , Phosphotransferases (Alcohol Group Acceptor)*/chemistry , 1-Phosphatidylinositol 4-Kinase*/metabolism , 1-Phosphatidylinositol 4-Kinase*/chemistry, Humans ; Protein Binding
Περίληψη: The armadillo repeat protein ARMH3 regulates the activity and localization of the Golgi resident lipid kinase phosphatidylinositol 4 kinase IIIβ (PI4KB) and the Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 (GBF1) that activates Arf1. ARMH3 localizes to the trans-Golgi network (TGN) via the GTPase Arl5. We used hydrogen deuterium exchange mass spectrometry (HDX-MS) and AI-enabled modeling to define the interfaces of ARMH3 with its binding partners Arl5, PI4KB, and GBF1. The ARMH3-Arl5 interface was determined to consist of regions near the N and C termini of ARMH3, with Arl5 binding causing allosteric conformational changes in ARMH3 located at a shared PI4KB/GBF1 interface. ARMH3 binds to PI4KB and GBF1 at this shared competitive interface, with GBF1 binding to ARMH3 through a disordered loop we have named the ARMH3-binding region (ABR). Both GBF1 and PI4KB can form ternary complexes with ARMH3-Arl5. The ARMH3 interfaces in PI4KB and GBF1 contain phosphosites, with the phosphomimetic mutation of GBF1 blocking complex formation. These findings provide new insights into the role of ARMH3 as a master coordinator of GTPase and phosphoinositide signaling at the Golgi/TGN.
(Copyright © 2026 The Authors. Published by Elsevier Inc. All rights reserved.)
Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
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Contributed Indexing: Keywords: ARMH3; Arl5; GBF1; GTPases; Golgi/TGN; PI4KB; hydrogen–deuterium exchange mass spectrometry
Substance Nomenclature: 0 (Guanine Nucleotide Exchange Factors)
0 (GBF1 protein, human)
EC 2.7.1.67 (PI4KB protein, human)
EC 3.6.5.2 (ADP-Ribosylation Factors)
EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor))
EC 2.7.1.67 (1-Phosphatidylinositol 4-Kinase)
Entry Date(s): Date Created: 20260629 Date Completed: 20260820 Latest Revision: 20260923
Update Code: 20260923
PubMed Central ID: PMC13427656
DOI: 10.1016/j.jbc.2026.113307
PMID: 42372921
Βάση Δεδομένων: MEDLINE
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  Label: Title
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  Data: ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.
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  Data: <searchLink fieldCode="AU" term="%22Scott+MK%22">Scott MK</searchLink>; School of Molecular Life Sciences, University of Victoria, Victoria, British Columbia, Canada.<br /><searchLink fieldCode="AU" term="%22Klynsoon+GCT%22">Klynsoon GCT</searchLink>; School of Molecular Life Sciences, University of Victoria, Victoria, British Columbia, Canada.<br /><searchLink fieldCode="AU" term="%22Walsh+EE%22">Walsh EE</searchLink>; School of Molecular Life Sciences, University of Victoria, Victoria, British Columbia, Canada.<br /><searchLink fieldCode="AU" term="%22Suresh+S%22">Suresh S</searchLink>; School of Molecular Life Sciences, University of Victoria, Victoria, British Columbia, Canada.<br /><searchLink fieldCode="AU" term="%22Nyvall+HG%22">Nyvall HG</searchLink>; Department of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, British Columbia, Canada.<br /><searchLink fieldCode="AU" term="%22Burke+JE%22">Burke JE</searchLink>; School of Molecular Life Sciences, University of Victoria, Victoria, British Columbia, Canada; Department of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, British Columbia, Canada; University of Victoria Genome BC Proteomics Centre, Victoria, British Columbia, Canada. Electronic address: jeburke@uvic.ca.
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  Data: <searchLink fieldCode="JN" term="%222985121R%22">The Journal of biological chemistry</searchLink> [J Biol Chem] 2026 Aug; Vol. 302 (8), pp. 113307. <i>Date of Electronic Publication: </i>2026 Jun 29.
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Elsevier+Inc%2E+on+behalf+of+American+Society+for+Biochemistry+and+Molecular+Biology%22">Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>2985121R <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1083-351X (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2200219258%22">00219258 </searchLink><i>NLM ISO Abbreviation: </i>J Biol Chem <i>Subsets: </i>MEDLINE
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  Data: <i>Publication</i>: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology<br /><i>Original Publication</i>: Baltimore, MD : American Society for Biochemistry and Molecular Biology
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  Data: <searchLink fieldCode="MM" term="%22Guanine+Nucleotide+Exchange+Factors%22">Guanine Nucleotide Exchange Factors*</searchLink>/<searchLink fieldCode="MM" term="%22Guanine+Nucleotide+Exchange+Factors+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Guanine+Nucleotide+Exchange+Factors%22">Guanine Nucleotide Exchange Factors*</searchLink>/<searchLink fieldCode="MM" term="%22Guanine+Nucleotide+Exchange+Factors+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Golgi+Apparatus%22">Golgi Apparatus*</searchLink>/<searchLink fieldCode="MM" term="%22Golgi+Apparatus+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22trans-Golgi+Network%22">trans-Golgi Network*</searchLink>/<searchLink fieldCode="MM" term="%22trans-Golgi+Network+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22ADP-Ribosylation+Factors%22">ADP-Ribosylation Factors*</searchLink>/<searchLink fieldCode="MM" term="%22ADP-Ribosylation+Factors+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22ADP-Ribosylation+Factors%22">ADP-Ribosylation Factors*</searchLink>/<searchLink fieldCode="MM" term="%22ADP-Ribosylation+Factors+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Phosphotransferases+%28Alcohol+Group+Acceptor%29%22">Phosphotransferases (Alcohol Group Acceptor)*</searchLink>/<searchLink fieldCode="MM" term="%22Phosphotransferases+%28Alcohol+Group+Acceptor%29+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Phosphotransferases+%28Alcohol+Group+Acceptor%29%22">Phosphotransferases (Alcohol Group Acceptor)*</searchLink>/<searchLink fieldCode="MM" term="%22Phosphotransferases+%28Alcohol+Group+Acceptor%29+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%221-Phosphatidylinositol+4-Kinase%22">1-Phosphatidylinositol 4-Kinase*</searchLink>/<searchLink fieldCode="MM" term="%221-Phosphatidylinositol+4-Kinase+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%221-Phosphatidylinositol+4-Kinase%22">1-Phosphatidylinositol 4-Kinase*</searchLink>/<searchLink fieldCode="MM" term="%221-Phosphatidylinositol+4-Kinase+chemistry%22">chemistry</searchLink><br /><searchLink fieldCode="MH" term="%22Humans%22">Humans</searchLink> ; <searchLink fieldCode="MH" term="%22Protein+Binding%22">Protein Binding</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: The armadillo repeat protein ARMH3 regulates the activity and localization of the Golgi resident lipid kinase phosphatidylinositol 4 kinase IIIβ (PI4KB) and the Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 (GBF1) that activates Arf1. ARMH3 localizes to the trans-Golgi network (TGN) via the GTPase Arl5. We used hydrogen deuterium exchange mass spectrometry (HDX-MS) and AI-enabled modeling to define the interfaces of ARMH3 with its binding partners Arl5, PI4KB, and GBF1. The ARMH3-Arl5 interface was determined to consist of regions near the N and C termini of ARMH3, with Arl5 binding causing allosteric conformational changes in ARMH3 located at a shared PI4KB/GBF1 interface. ARMH3 binds to PI4KB and GBF1 at this shared competitive interface, with GBF1 binding to ARMH3 through a disordered loop we have named the ARMH3-binding region (ABR). Both GBF1 and PI4KB can form ternary complexes with ARMH3-Arl5. The ARMH3 interfaces in PI4KB and GBF1 contain phosphosites, with the phosphomimetic mutation of GBF1 blocking complex formation. These findings provide new insights into the role of ARMH3 as a master coordinator of GTPase and phosphoinositide signaling at the Golgi/TGN.<br /> (Copyright © 2026 The Authors. Published by Elsevier Inc. All rights reserved.)
– Name: Abstract
  Label: Competing Interests
  Group: Ab
  Data: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
– Name: Ref
  Label: References
  Group: RefInfo
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(PMID: <searchLink fieldCode="PM" term="%2233877613%22">33877613)</searchLink><br />J Am Soc Mass Spectrom. 2020 Oct 7;31(10):2202-2209. (PMID: <searchLink fieldCode="PM" term="%2232869988%22">32869988)</searchLink><br />J Cell Sci. 2007 Nov 15;120(Pt 22):3929-40. (PMID: <searchLink fieldCode="PM" term="%2217956946%22">17956946)</searchLink><br />Nat Cell Biol. 1999 Sep;1(5):280-7. (PMID: <searchLink fieldCode="PM" term="%2210559940%22">10559940)</searchLink><br />Front Cell Dev Biol. 2023 Sep 07;11:1233272. (PMID: <searchLink fieldCode="PM" term="%2237745300%22">37745300)</searchLink><br />Nat Methods. 2020 Sep;17(9):869-870. (PMID: <searchLink fieldCode="PM" term="%2232669682%22">32669682)</searchLink><br />Nat Methods. 2017 May;14(5):513-520. (PMID: <searchLink fieldCode="PM" term="%2228394336%22">28394336)</searchLink><br />Biochem Soc Trans. 2016 Feb;44(1):260-6. 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(PMID: <searchLink fieldCode="PM" term="%2234493042%22">34493042)</searchLink><br />Biochem Biophys Res Commun. 2005 Jul 8;332(3):640-5. (PMID: <searchLink fieldCode="PM" term="%2215896705%22">15896705)</searchLink><br />Nature. 2024 May;629(8014):1174-1181. (PMID: <searchLink fieldCode="PM" term="%2238720073%22">38720073)</searchLink><br />Mol Cell Proteomics. 2019 Nov;18(11):2285-2297. (PMID: <searchLink fieldCode="PM" term="%2231519766%22">31519766)</searchLink><br />Mol Cell. 2018 Sep 6;71(5):653-673. (PMID: <searchLink fieldCode="PM" term="%2230193094%22">30193094)</searchLink><br />Structure. 2017 Jan 3;25(1):121-131. (PMID: <searchLink fieldCode="PM" term="%2227989622%22">27989622)</searchLink><br />Nucleic Acids Res. 2022 Jan 7;50(D1):D543-D552. (PMID: <searchLink fieldCode="PM" term="%2234723319%22">34723319)</searchLink><br />Trends Microbiol. 2016 Jul;24(7):535-546. (PMID: <searchLink fieldCode="PM" term="%2227020598%22">27020598)</searchLink><br />J Virol. 2009 Nov;83(22):11940-9. (PMID: <searchLink fieldCode="PM" term="%2219740986%22">19740986)</searchLink><br />Nat Methods. 2009 May;6(5):343-5. (PMID: <searchLink fieldCode="PM" term="%2219363495%22">19363495)</searchLink><br />Annu Rev Cell Dev Biol. 2009;25:113-32. (PMID: <searchLink fieldCode="PM" term="%2219575639%22">19575639)</searchLink><br />Mol Biol Cell. 2008 Feb;19(2):523-35. (PMID: <searchLink fieldCode="PM" term="%2218003980%22">18003980)</searchLink><br />Nat Rev Mol Cell Biol. 2019 Feb;20(2):85-101. (PMID: <searchLink fieldCode="PM" term="%2230337668%22">30337668)</searchLink>
– Name: SubjectMinor
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  Data: <i>Keywords: </i>ARMH3; Arl5; GBF1; GTPases; Golgi/TGN; PI4KB; hydrogen–deuterium exchange mass spectrometry
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  Data: 0 (Guanine Nucleotide Exchange Factors)<br />0 (GBF1 protein, human)<br />EC 2.7.1.67 (PI4KB protein, human)<br />EC 3.6.5.2 (ADP-Ribosylation Factors)<br />EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor))<br />EC 2.7.1.67 (1-Phosphatidylinositol 4-Kinase)
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      – SubjectFull: Protein Binding
        Type: general
      – SubjectFull: Guanine Nucleotide Exchange Factors metabolism
        Type: general
      – SubjectFull: Guanine Nucleotide Exchange Factors chemistry
        Type: general
      – SubjectFull: Golgi Apparatus metabolism
        Type: general
      – SubjectFull: trans-Golgi Network metabolism
        Type: general
      – SubjectFull: ADP-Ribosylation Factors metabolism
        Type: general
      – SubjectFull: ADP-Ribosylation Factors chemistry
        Type: general
      – SubjectFull: Phosphotransferases (Alcohol Group Acceptor) metabolism
        Type: general
      – SubjectFull: Phosphotransferases (Alcohol Group Acceptor) chemistry
        Type: general
      – SubjectFull: 1-Phosphatidylinositol 4-Kinase metabolism
        Type: general
      – SubjectFull: 1-Phosphatidylinositol 4-Kinase chemistry
        Type: general
    Titles:
      – TitleFull: ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Scott MK
      – PersonEntity:
          Name:
            NameFull: Klynsoon GCT
      – PersonEntity:
          Name:
            NameFull: Walsh EE
      – PersonEntity:
          Name:
            NameFull: Suresh S
      – PersonEntity:
          Name:
            NameFull: Nyvall HG
      – PersonEntity:
          Name:
            NameFull: Burke JE
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 08
              Text: 2026 Aug
              Type: published
              Y: 2026
          Identifiers:
            – Type: issn-electronic
              Value: 1083-351X
          Numbering:
            – Type: volume
              Value: 302
            – Type: issue
              Value: 8
          Titles:
            – TitleFull: The Journal of biological chemistry
              Type: main
ResultId 1