Recruitment of the inhibitor Cand1 to the cullin substrate adaptor site mediates interaction to the neddylation site

Helmstaedt, Kerstin; Schwier, Elke U.; Christmann, Martin; Nahlik, Krystyna; Westermann, Mieke; Harting, Rebekka; Grond, Stephanie; Busch, Silke; Braus, Gerhard H.

doi:10.1091/mbc.e10-08-0732

Cited by 28 publications

(32 citation statements)

References 58 publications

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“…The denA/csnE double mutant combines the phenotypes of a Δ denA strain which forms only marginal amounts of asexual spores and of Δ csnE which is unable to produce sexual fruit bodies. The closest phenotype, reminiscent to the Δ csnE/ΔdenA strain, has been recently described for CandA [9], the fungal homolog of human Cullin-associated Nedd8-dissociated protein 1 (CAND1) [52]. In general, CAND1 interaction only occurs to non-neddylated cullins and requires deneddylation as prerequisite [52], [53].…”

Section: Discussionmentioning

confidence: 95%

“…This suggests an interaction of DenA with the CSN complex. Bi-molecular fluorescence complementation (BiFC) studies [9] were conducted to verify the major interaction of DenA with the CsnG/CSN7 subunit. DenA and CsnG/CSN7 were fused to one half of a split yellow fluorescent protein (YFP) at their N-termini.…”

Section: Resultsmentioning

confidence: 99%

“…Defects in CAND1 can lead to increased stability of certain types of SCF ligase complexes while the formation of others is abolished [10]. This might explain why, in A. nidulans , the defects in sexual differentiation and secondary metabolism of a csnE deletion mutant [14], [45], as well as the asexual phenotype of the denA deletion strain appear not only in the corresponding double deletion mutant, but also in the fungal candA mutants [9]. It is also an indication that both the CSN complex and DenA act in a similar pathway which might converge at the molecular level at the conserved physical interaction of both deneddylases.…”

Section: Discussionmentioning

confidence: 99%

“…Deneddylation of cullins inactivates CRLs and allows the disassembly of the enzyme complex and the binding of CAND1 (Cullin associated Nedd8 dissociated protein 1) [8], [9]. CAND1 is important for the reassembly of E3 complexes [10].…”

Section: Introductionmentioning

confidence: 99%

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Control of Multicellular Development by the Physically Interacting Deneddylases DEN1/DenA and COP9 Signalosome

et al. 2013

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Deneddylases remove the ubiquitin-like protein Nedd8 from modified proteins. An increased deneddylase activity has been associated with various human cancers. In contrast, we show here that a mutant strain of the model fungus Aspergillus nidulans deficient in two deneddylases is viable but can only grow as a filament and is highly impaired for multicellular development. The DEN1/DenA and the COP9 signalosome (CSN) deneddylases physically interact in A. nidulans as well as in human cells, and CSN targets DEN1/DenA for protein degradation. Fungal development responds to light and requires both deneddylases for an appropriate light reaction. In contrast to CSN, which is necessary for sexual development, DEN1/DenA is required for asexual development. The CSN-DEN1/DenA interaction that affects DEN1/DenA protein levels presumably balances cellular deneddylase activity. A deneddylase disequilibrium impairs multicellular development and suggests that control of deneddylase activity is important for multicellular development.

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Section: Discussionmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Control of Multicellular Development by the Physically Interacting Deneddylases DEN1/DenA and COP9 Signalosome

et al. 2013

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“…SUMO is required for sexual development in A. nidulans, where the COMPASS histone 3 lysine 4 methyltransferase complex connects the SUMO network to histone modifications (378). The ubiquitin-like protein Nedd8 controls various cullin E3 ubiquitin ligases and the incorporation of F-box proteins as substrate receptors, which is important to control the ratio between sexual and asexual differentiation (379)(380)(381). The multiprotein complex COP9 signalosome represents a deneddylase, which removes Nedd8 and is involved in the coordination of sexual development and secondary metabolism.…”

Section: Fruiting Body Formationmentioning

confidence: 99%

Fungal Morphogenesis, from the Polarized Growth of Hyphae to Complex Reproduction and Infection Structures

Riquelme

Aguirre

Bartnicki-García

et al. 2018

Microbiol Mol Biol Rev

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273

246

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SUMMARYFilamentous fungi constitute a large group of eukaryotic microorganisms that grow by forming simple tube-like hyphae that are capable of differentiating into more-complex morphological structures and distinct cell types. Hyphae form filamentous networks by extending at their tips while branching in subapical regions. Rapid tip elongation requires massive membrane insertion and extension of the rigid chitin-containing cell wall. This process is sustained by a continuous flow of secretory vesicles that depends on the coordinated action of the microtubule and actin cytoskeletons and the corresponding motors and associated proteins. Vesicles transport cell wall-synthesizing enzymes and accumulate in a special structure, the Spitzenkörper, before traveling further and fusing with the tip membrane. The place of vesicle fusion and growth direction are enabled and defined by the position of the Spitzenkörper, the so-called cell end markers, and other proteins involved in the exocytic process. Also important for tip extension is membrane recycling by endocytosis via early endosomes, which function as multipurpose transport vehicles for mRNA, septins, ribosomes, and peroxisomes. Cell integrity, hyphal branching, and morphogenesis are all processes that are largely dependent on vesicle and cytoskeleton dynamics. When hyphae differentiate structures for asexual or sexual reproduction or to mediate interspecies interactions, the hyphal basic cellular machinery may be reprogrammed through the synthesis of new proteins and/or the modification of protein activity. Although some transcriptional networks involved in such reprogramming of hyphae are well studied in several model filamentous fungi, clear connections between these networks and known determinants of hyphal morphogenesis are yet to be established.

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8 Coordination of Fungal Secondary Metabolism and Development

Gerke

Köhler

Meister

et al. 2020

Genetics and Biotechnology

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Recruitment of the inhibitor Cand1 to the cullin substrate adaptor site mediates interaction to the neddylation site

Abstract: Cand1 can be separated into two functional polypeptides. C-terminal Cand1 binds first at the cullin adaptor site. N-terminal Cand1 blocks the neddylation site subsequently. Defects in the split fungal Cand1 impair development more than defects in CSN.

Cited by 28 publications

References 58 publications

Control of Multicellular Development by the Physically Interacting Deneddylases DEN1/DenA and COP9 Signalosome

Control of Multicellular Development by the Physically Interacting Deneddylases DEN1/DenA and COP9 Signalosome

Fungal Morphogenesis, from the Polarized Growth of Hyphae to Complex Reproduction and Infection Structures

8 Coordination of Fungal Secondary Metabolism and Development

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