Affinage

CCZ1

Vacuolar fusion protein CCZ1 homolog · UniProt P86791

Length
482 aa
Mass
55.9 kDa
Annotated
2026-06-09
29 papers in source corpus 19 papers cited in narrative 19 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/8 claims corpus-supported (88%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CCZ1 is an obligate subunit of a membrane-trafficking guanine nucleotide exchange factor (GEF) that drives endosomal maturation and autophagosome-lysosome fusion by activating the late-endosomal Rab7/Ypt7 GTPase (PMID:20797862, PMID:12364329). CCZ1 forms a stable heterodimer with MON1, and only the assembled complex—not either protein alone—catalyzes nucleotide exchange on Ypt7, counteracts GAP activity, and rescues vacuole fusion (PMID:20797862); CCZ1 itself contacts the substrate GTPase Ypt7 directly (PMID:11590240). The complex acts at the tethering/docking stage of homotypic fusion, where its membrane association is governed by the HOPS/class C Vps machinery (PMID:14662743). Membrane recruitment follows a synergistic code: binding to PI3P (PMID:24623720), an autophagy-specific LIR motif in the CCZ1 C-terminus that engages Atg8/LC3 to target pre-autophagosomal structures (PMID:29446751), and a CCZ1 amphipathic helix that reads lipid-packing defects and selectively supports autophagy over endosomal maturation (PMID:36649906). After activating Rab7, MON1 is phosphorylated by the casein kinase Yck3, releasing the complex from the membrane for recycling (PMID:24623720). In metazoans the complex acquires a third subunit, RMC1/Bulli, which forms a peripheral leg-like extension serving as a recruitment platform and contributing electrostatic membrane binding without altering core GEF catalysis (PMID:29038162, PMID:37155863, PMID:40864718). The complex functions across endosomal maturation, autophagy, mitophagy, and phagosome maturation (PMID:27559127, PMID:26627821, PMID:34432599, PMID:20519582), and CCZ1 is an essential host factor for early-to-late endosomal trafficking of Ebola and Marburg filoviruses (PMID:37880247). Restoring CCZ1-MON1A activity enhances Rab7-dependent autophagosome maturation and clearance of APP-CTFs, Aβ, and P-tau in Alzheimer's disease models (PMID:35198070).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 2001 Medium

    Establishing that CCZ1 physically engages the Rab GTPase Ypt7 connected the previously orphan CCZ1 to Rab7-dependent membrane fusion.

    Evidence suppressor genetics mapping CCZ1-deletion suppressors to YPT7 alleles, plus co-immunoprecipitation in yeast

    PMID:11590240

    Open questions at the time
    • Did not establish whether CCZ1 acts catalytically on Ypt7 or merely binds it
    • Role of a CCZ1 partner not yet defined
  2. 2002 High

    Defining MON1 and CCZ1 as a stable complex acting after vesicle formation but before vacuolar fusion placed the complex at a discrete trafficking step across multiple pathways.

    Evidence reciprocal Co-IP, subcellular fractionation, and deletion analysis across Cvt, autophagy, pexophagy and MVB/CPY/ALP pathways in yeast

    PMID:12364329

    Open questions at the time
    • Molecular activity of the complex not yet identified
    • Mechanism of perivacuolar recruitment unknown
  3. 2003 High

    Localizing CCZ1-MON1 function to the tethering/docking stage of homotypic fusion tied the complex to SNARE pairing and HOPS-regulated membrane association.

    Evidence in vitro homotypic vacuole fusion assay, SNARE Co-IP, and co-localization in yeast

    PMID:14662743

    Open questions at the time
    • Did not yet define the biochemical activity (GEF) underlying the fusion defect
    • Causal order between HOPS and CCZ1-MON1 incompletely resolved
  4. 2010 High

    Reconstituting GEF activity demonstrated that the MON1-CCZ1 dimer—not either protein alone—is the nucleotide exchange factor for Ypt7/Rab7, defining the complex's core biochemical function.

    Evidence in vitro nucleotide exchange assay, in vitro vacuole fusion rescue, and in vivo GAP suppression; parallel C. elegans phagosome maturation genetics

    PMID:20519582 PMID:20797862

    Open questions at the time
    • Did not address how the complex is targeted to specific membranes
    • Did not resolve autophagy- versus endosome-specific functions
  5. 2014 High

    Identifying PI3P binding and Yck3-dependent phosphorylation revealed how the GEF is recruited to and subsequently released from membranes, defining a recruitment-recycling cycle.

    Evidence PI3P lipid competition, recombinant Yck3 add-back, and phosphomutant membrane-binding assays in yeast

    PMID:24623720

    Open questions at the time
    • Did not explain how recruitment is made autophagy-specific
    • Phospho-regulation tested in yeast only
  6. 2015 Medium

    FRET sensing in mammalian cells showed MON1-CCZ1 activates Rab7 specifically on late endosomes, with lysosomal Rab7 activity controlled by a distinct, complex-independent mechanism, refining the spatial logic of Rab7 activation.

    Evidence FRET-based Rab7 biosensor with siRNA knockdown and EGF-induced macropinocytosis in mammalian cells

    PMID:26627821

    Open questions at the time
    • The MON1-CCZ1-independent lysosomal Rab7 activator not identified
    • Single biosensor approach in one lab
  7. 2016 Medium

    Drosophila genetics positioned the CCZ1-MON1-Rab7 module downstream of PI3P generation and upstream of autophagosome-lysosome fusion, independent of Rab5.

    Evidence loss-of-function mutants, autophagosome quantification, and epistasis in fly fat cells

    PMID:27559127

    Open questions at the time
    • Did not define the molecular recruiter linking PI3P-positive autophagosomes to the complex
  8. 2017 Medium

    Discovery of RMC1/C18orf8 as a metazoan-specific subunit expanded the dimeric GEF into a trimeric complex that promotes Rab7 recruitment.

    Evidence interaction proteomics from GABARAP/L1/L2-deficient cells and functional validation in ATG8 knockouts

    PMID:29038162

    Open questions at the time
    • Structural placement and catalytic contribution of RMC1 not yet defined
  9. 2018 High

    Defining a CCZ1 LIR motif that binds Atg8 explained how the complex is targeted specifically to pre-autophagosomal structures, separating autophagic from endosomal recruitment.

    Evidence LIR mutagenesis, in vitro binding and GEF assays, and microscopy in yeast

    PMID:29446751

    Open questions at the time
    • Whether LIR-mediated targeting operates identically in metazoans not established
  10. 2021 Medium

    Identifying C5orf51 as a complex component linked MON1-CCZ1 to RAB7A stabilization and mitochondrial recruitment during mitophagy.

    Evidence miniTurbo proximity biotinylation with GDP-locked RAB7A, Co-IP, and knockout phenotyping in mammalian cells

    PMID:34432599

    Open questions at the time
    • Relationship between C5orf51 and RMC1 within the complex unclear
    • Single lab
  11. 2022 Medium

    Mapping the V-ATPase a3 interaction and demonstrating CCZ1-MON1A's role in Alzheimer's models connected the GEF to organelle-specific recruitment and to neurodegenerative proteostasis.

    Evidence Co-IP with domain mapping in HEK293T and a3-knockout osteoclasts; autophagosome fractionation and AAV overexpression in mouse brain

    PMID:35198070 PMID:35589873

    Open questions at the time
    • Direct GEF deficit in disease vs. compensatory effect not fully separated
    • Longin-domain/a3 interaction tested in limited cell types
  12. 2023 High

    Cryo-EM of the trimeric MCBulli complex and dissection of the CCZ1 amphipathic helix resolved the architecture and the dual lipid-/recruiter-based membrane code that distinguishes autophagic from endosomal targeting.

    Evidence 3.2 Å cryo-EM, lipid-binding and in vitro GEF assays with mutagenesis, plus a haploid screen identifying CCZ1 as an essential filovirus host factor

    PMID:36649906 PMID:37155863 PMID:37880247

    Open questions at the time
    • Regulators recruited via the Bulli leg not identified
    • How amphipathic helix and PI3P binding are coordinated in vivo unresolved
  13. 2025 High

    Comparative structural and biochemical analysis showed tri-longin GEFs share a conserved substrate-recognition motif while secondary interactions confer target specificity, and that metazoan RMC1/Bulli supplies electrostatic membrane recruitment through a distinct interface.

    Evidence structural determination, protein-lipid interaction assays, in vitro reconstitution, and Drosophila functional genetics

    PMID:40864718

    Open questions at the time
    • Full set of secondary interactions governing in vivo specificity not enumerated
  14. 2026 Medium

    Demonstrating that Rab5 directly stimulates the trimeric Rab7 GEF positioned the complex within a Rab5-to-Rab7 conversion switch during endosomal maturation.

    Evidence Drosophila nephrocyte genetics, trafficking microscopy, and biochemical GEF-stimulation analysis

    PMID:41943871

    Open questions at the time
    • Mechanistic basis of Rab5-mediated GEF stimulation not structurally defined
    • Single study

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the distinct recruitment modules (PI3P, Atg8/LIR, amphipathic helix, RMC1/Bulli electrostatics, V-ATPase a3, Rab5) are integrated to select among endosomal, autophagic, mitophagic, and phagosomal targets in a single cell remains unresolved.
  • No unified in vivo model of compartment-selective recruitment
  • Regulators docking on the Bulli platform unidentified
  • Mammalian counterpart of Yck3 phospho-recycling not characterized in the corpus

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0008289 lipid binding 3 GO:0140096 catalytic activity, acting on a protein 3 GO:0098772 molecular function regulator activity 2
Localization
GO:0005764 lysosome 2 GO:0005768 endosome 2 GO:0005773 vacuole 2
Pathway
R-HSA-9612973 Autophagy 4 R-HSA-5653656 Vesicle-mediated transport 3 R-HSA-9609507 Protein localization 2
Partners
ATG8C5ORF51MON1RAB7ARMC1TCIRG1YPT7
Complex memberships
MON1-CCZ1 GEF complexMON1-CCZ1-RMC1/Bulli (MCBulli) trimeric complex

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2010 The dimeric Mon1-Ccz1 complex is the guanine nucleotide exchange factor (GEF) for the late endosomal Rab7 homolog Ypt7. The complex, but neither protein alone, counteracts GAP function in vivo, rescues in vitro fusion of vacuoles carrying Ypt7-GDP, and promotes nucleotide exchange on Ypt7 independently of Vps39/HOPS. In vitro nucleotide exchange assay, in vitro vacuole fusion assay, in vivo GAP suppression assay Current biology : CB High 20797862
2002 Mon1 and Ccz1 physically interact as a stable protein complex (the Ccz1-Mon1 complex), function in nearly all membrane-trafficking pathways targeting the vacuole, and act after transport vesicle formation but before or at the fusion step with the vacuole. The complex peripherally associates with a perivacuolar compartment. Co-immunoprecipitation, subcellular fractionation, fluorescence microscopy, genetic deletion analysis with multiple pathway readouts (Cvt, autophagy, pexophagy, CPY/ALP/MVB pathways) The Journal of biological chemistry High 12364329
2003 The Ccz1-Mon1 complex is required for the tethering/docking stage of homotypic vacuole fusion. In its absence, SNARE pairing integrity and the class C Vps/HOPS complex interaction with unpaired SNAREs are both impaired. The complex co-localizes with other fusion components on the vacuole as part of the cis-SNARE complex, and its vacuolar association is regulated by the class C Vps/HOPS complex. In vitro homotypic vacuole fusion assay, SNARE co-immunoprecipitation, fluorescence co-localization, genetic analysis The Journal of cell biology High 14662743
2001 Ccz1 physically interacts with the Rab GTPase Ypt7. Extragenic suppressors of CCZ1 deletion all mapped to mutated alleles of YPT7 (with mutations in the guanine-binding domains), and direct physical interaction was confirmed by co-immunoprecipitation. Suppressor genetics, co-immunoprecipitation Journal of cell science Medium 11590240
2014 Mon1-Ccz1 is recruited to endosomes and vacuoles through binding to phosphatidylinositol 3-phosphate (PI3P). After activating Ypt7, Mon1 is phosphorylated by the type 1 casein kinase Yck3 and released from vacuoles for recycling. Phosphorylation-site mutants of Mon1 are retained on vacuoles, and this retention is rescued by addition of recombinant Yck3. Lipid competition assay (PI3P), recombinant kinase add-back assay, phosphomutant analysis, vacuole membrane binding assay Molecular biology of the cell High 24623720
2018 Mon1-Ccz1 is specifically recruited to the pre-autophagosomal structure under starvation by directly binding Atg8 (yeast LC3 homolog) via at least one LIR motif in the Ccz1 C-terminus. This LIR motif is essential for autophagy but not for endosomal transport. Only wild-type, not LIR-mutated Mon1-Ccz1, promotes Atg8-dependent activation of Ypt7. LIR motif mutagenesis, in vitro binding assay, GEF activity assay, fluorescence microscopy, yeast genetics eLife High 29446751
2016 The Ccz1-Mon1-Rab7 module is required for autophagosome-lysosome fusion in Drosophila fat cells. Rab5 is dispensable for the Ccz1-Mon1-dependent recruitment of Rab7 to PI3P-positive autophagosomes (which are generated by Atg14-containing Vps34 PI3 kinase complex), placing the Ccz1-Mon1 complex downstream of PI3P generation and upstream of autophagosome-lysosome fusion. Genetic loss-of-function (Drosophila mutants), fluorescence microscopy, autophagosome quantification, epistasis analysis Molecular biology of the cell Medium 27559127
2015 Mon1-Ccz1 activates Rab7 specifically on late endosomes in mammalian cells; Rab7 activity on lysosomes is independent of Mon1-Ccz1. Mon1-Ccz1 dissociates from lysosomes after late endosome-lysosome fusion. Active Rab7 on lysosomes (independent of Mon1-Ccz1) plays a role in perinuclear lysosome clustering. FRET-based Rab7 activity sensor, confocal FRET imaging, siRNA knockdown of Mon1-Ccz1, EGF-induced macropinocytosis assay Journal of cell science Medium 26627821
2017 C18orf8/RMC1 is a new subunit of the CCZ1-MON1 RAB7 guanine exchange factor complex and positively regulates RAB7 recruitment to late endosomes/autophagosomes. This was identified through interaction proteomics of proteins accumulating in GABARAP/L1/L2-deficient cells. Interaction proteomics (AP-MS), genetic cell engineering (ATG8 knockouts), quantitative autophagosome proteomics Molecular and cellular biology Medium 29038162
2021 C5orf51 is a component of the MON1-CCZ1 complex, identified as an interactor of GDP-locked RAB7A by proximity biotinylation. In the absence of C5orf51, RAB7A localization on depolarized mitochondria is compromised and RAB7A is degraded by the proteasome, indicating C5orf51 stabilizes RAB7A and supports its mitochondrial recruitment during mitophagy. Proximity-dependent biotinylation (miniTurbo), co-immunoprecipitation, knockout cell analysis, fluorescence microscopy Autophagy Medium 34432599
2022 The lysosomal V-ATPase a3 subunit interacts with the Mon1A-Ccz1 complex (GEF for Rab7) via the amino-terminal half domain of a3 and the longin motifs of Mon1A and Ccz1. This interaction is required for Mon1A-Ccz1 localization to secretory lysosomes in osteoclasts, which mediates Rab7 recruitment to the organelle. Co-immunoprecipitation in HEK293T cells, domain mapping by truncation mutants, endogenous Ccz1 localization analysis in a3-knockout osteoclasts Scientific reports Medium 35589873
2023 Cryo-EM structure of the metazoan Mon1-Ccz1-Bulli (MCBulli) complex was solved at 3.2 Å resolution. Bulli associates as a leg-like extension at the periphery of the Mon1-Ccz1 heterodimer and does not impact GEF activity or interactions with recruiter/substrate GTPases, but likely serves as a recruitment platform for additional regulators of endolysosomal trafficking. Cryo-electron microscopy (3.2 Å), structural analysis Proceedings of the National Academy of Sciences of the United States of America High 37155863
2023 An amphipathic helix in Ccz1 is required for Mon1-Ccz1 function in autophagy but not endosomal maturation, revealing a mechanism for differential targeting to autophagosomes vs. endosomes. The Ccz1 amphipathic helix interacts with lipid packing defects, Mon1 basic patches bind positively charged lipids, and association with recruiter proteins synergistically governs membrane recruitment. Interaction with recruiter proteins can further stimulate GEF activity beyond membrane concentration effects. Mutagenesis, lipid-binding assays, in vitro GEF activity assays, yeast functional genetics The Journal of biological chemistry High 36649906
2023 CCZ1 controls early-to-late endosomal trafficking of Marburg and Ebola filoviruses, functioning as an essential host factor in the early stage of filovirus replication. Loss of CCZ1 nearly completely abolishes Marburg and Ebola infections, validated in 3D primary human hepatocyte cultures and blood-vessel organoids. Haploid cell genetic screen, CCZ1 knockout validation, 3D primary human tissue models (hepatocyte cultures, blood-vessel organoids), viral infection assays Nature communications Medium 37880247
2022 CCZ1-MON1A complex dysfunction causes decreased active RAB7 on autophagosome fractions in Alzheimer's disease models. Overexpressing CCZ1-MON1A increases active RAB7, enhances autophagosome maturation, and promotes degradation of APP-CTFs, Aβ, and P-tau in an autophagy-dependent manner. Autophagosome fractionation, GST-R7BD affinity isolation assay for GTP-RAB7, AAV-mediated overexpression in mouse brain, immunoblotting Theranostics Medium 35198070
2025 Structural and biochemical comparison of Mon1-Ccz1 and Fuzzy-Inturned reveals that both tri-longin domain GEF complexes use a conserved sequence motif of their substrate GTPases for catalysis, while secondary interactions mediate target discrimination. The metazoan RMC1/Bulli subunit mediates membrane recruitment of the Mon1-Ccz1 GEF complex via electrostatic interactions through a distinct interface from the fungal dimer, demonstrated by protein-lipid interaction studies and functional characterization in flies. Structural determination, protein-lipid interaction assays, in vitro reconstitution, functional genetics in Drosophila Science advances High 40864718
2010 In C. elegans, CCZ-1 mediates digestion of apoptotic corpses by acting in phagosome maturation through recruitment of the GTPase RAB-7 to phagosomes, placing CCZ-1 upstream of RAB-7 in the phagosome maturation pathway. Genetic loss-of-function (C. elegans deletion mutants), fluorescence microscopy of corpse persistence and RAB-7 recruitment Journal of cell science Medium 20519582
2014 In C. elegans, CCZ-1 functions independently of SAND-1 (Mon1 ortholog) in gut granule (lysosome-related organelle) biogenesis, possibly acting with GLO-3 as a GEF for the Rab32/38-related GTPase GLO-1. Point mutations in GLO-1 predicted to increase spontaneous nucleotide exchange suppress loss of gut granules by ccz-1 mutants, genetically placing CCZ-1 upstream of GLO-1. Genetic epistasis (suppressor analysis), fluorescence microscopy, C. elegans mutant analysis Molecular biology of the cell Low 24501423
2026 The trimeric Bulli-Mon1-Ccz1 Rab7 GEF complex (BuMC1-GEF) interacts with Rab5, which stimulates its GEF activity during endosomal maturation in Drosophila nephrocytes. GAPsec is identified as a GAP for Rab5 required for endosomal maturation; its inactivation results in enlarged dysfunctional endosomes unable to fuse with lysosomes. Drosophila genetic loss-of-function, fluorescence microscopy of endosomal trafficking, biochemical interaction analysis Journal of cell science Medium 41943871

Source papers

Stage 0 corpus · 29 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2010 The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog Ypt7. Current biology : CB 319 20797862
2016 The Ccz1-Mon1-Rab7 module and Rab5 control distinct steps of autophagy. Molecular biology of the cell 169 27559127
2017 Systematic Analysis of Human Cells Lacking ATG8 Proteins Uncovers Roles for GABARAPs and the CCZ1/MON1 Regulator C18orf8/RMC1 in Macroautophagic and Selective Autophagic Flux. Molecular and cellular biology 105 29038162
2002 The Ccz1-Mon1 protein complex is required for the late step of multiple vacuole delivery pathways. The Journal of biological chemistry 104 12364329
2003 Yeast homotypic vacuole fusion requires the Ccz1-Mon1 complex during the tethering/docking stage. The Journal of cell biology 94 14662743
2018 Molecular mechanism to target the endosomal Mon1-Ccz1 GEF complex to the pre-autophagosomal structure. eLife 77 29446751
2014 Dynamic association of the PI3P-interacting Mon1-Ccz1 GEF with vacuoles is controlled through its phosphorylation by the type 1 casein kinase Yck3. Molecular biology of the cell 51 24623720
2001 The Ccz1 protein interacts with Ypt7 GTPase during fusion of multiple transport intermediates with the vacuole in S. cerevisiae. Journal of cell science 46 11590240
2015 Mon1-Ccz1 activates Rab7 only on late endosomes and dissociates from the lysosome in mammalian cells. Journal of cell science 40 26627821
2021 C5orf51 is a component of the MON1-CCZ1 complex and controls RAB7A localization and stability during mitophagy. Autophagy 35 34432599
2016 MONENSIN SENSITIVITY1 (MON1)/CALCIUM CAFFEINE ZINC SENSITIVITY1 (CCZ1)-Mediated Rab7 Activation Regulates Tapetal Programmed Cell Death and Pollen Development. Plant physiology 31 27799422
2010 ccz-1 mediates the digestion of apoptotic corpses in C. elegans. Journal of cell science 31 20519582
2021 Post-Golgi trafficking of rice storage proteins requires the small GTPase Rab7 activation complex MON1-CCZ1. Plant physiology 28 33871646
2022 Enhancing autophagy maturation with CCZ1-MON1A complex alleviates neuropathology and memory defects in Alzheimer disease models. Theranostics 26 35198070
2014 Caenorhabditis elegans HOPS and CCZ-1 mediate trafficking to lysosome-related organelles independently of RAB-7 and SAND-1. Molecular biology of the cell 22 24501423
2023 Targeting of the Mon1-Ccz1 Rab guanine nucleotide exchange factor to distinct organelles by a synergistic protein and lipid code. The Journal of biological chemistry 19 36649906
2015 The Ccz1 mediates the autophagic clearance of damaged mitochondria in response to oxidative stress in Candida albicans. The international journal of biochemistry & cell biology 18 26471407
2022 The lysosomal V-ATPase a3 subunit is involved in localization of Mon1-Ccz1, the GEF for Rab7, to secretory lysosomes in osteoclasts. Scientific reports 16 35589873
2010 Mutants of the Saccharomyces cerevisiae VPS genes CCZ1 and YPT7 are blocked in different stages of sporulation. European journal of cell biology 16 20709422
2023 Structure of the metazoan Rab7 GEF complex Mon1-Ccz1-Bulli. Proceedings of the National Academy of Sciences of the United States of America 15 37155863
2023 Identification of CCZ1 as an essential lysosomal trafficking regulator in Marburg and Ebola virus infections. Nature communications 12 37880247
2011 CCZ1, MON1 and YPT7 genes are involved in pexophagy, the Cvt pathway and non-specific macroautophagy in the methylotrophic yeast Pichia pastoris. Cell biology international 12 21155714
2024 The MON1-CCZ1 complex plays dual roles in autophagic degradation and vacuolar protein transport in rice. Journal of integrative plant biology 9 39474758
2004 The yeast genes, ARL1 and CCZ1, interact to control membrane traffic and ion homeostasis. Biochemical and biophysical research communications 7 15184059
2009 Mutations in the Saccharomyces cerevisiae vacuolar fusion proteins Ccz1, Mon1 and Ypt7 cause defects in cell cycle progression in a num1Delta background. European journal of cell biology 5 19700218
2022 VmMon1-Ccz1 Complex Is Required for Conidiation, Autophagy, and Virulence in Valsa mali. Molecular plant-microbe interactions : MPMI 3 35793146
2024 CCZ1 Accelerates the Progression of Cervical Squamous Cell Carcinoma by Promoting MMP2/MMP17 Expression. Biomedicines 2 39062041
2025 Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned. Science advances 1 40864718
2026 Endosomal maturation is controlled by the trimeric Bulli-Mon1-Ccz1 Rab7 GEF complex and the Rab5 GTPase-activating protein GAPsec. Journal of cell science 0 41943871

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