The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
SUP-17 (gene name: sup-17, ORF: DY3.7, UniProt: G5EFD9) is the Caenorhabditis elegans ortholog of mammalian ADAM10 (A Disintegrin And Metalloprotease 10), a highly conserved membrane-anchored zinc metalloprotease (white2005theadamfamily pages 98-102, seals2003theadamsfamily pages 2-4). The gene encodes a precursor protein that is processed to a mature enzyme responsible for ectodomain shedding of transmembrane protein substrates (saintpol2017regulationofthe pages 15-20, wang2018dissectingtherole pages 22-28). SUP-17 is classified under EC 3.4.24.81 and belongs to the ADAM family of multidomain metalloproteases that regulate cell behavior through proteolytic modification of cell-surface proteins (white2005theadamfamily pages 98-102, seals2003theadamsfamily pages 2-4).
SUP-17 is synthesized as an inactive precursor (zymogen) and undergoes maturation through the secretory pathway (white2005theadamfamily pages 98-102, seals2003theadamsfamily pages 4-5). The protein exhibits the canonical ADAM-family architecture consisting of the following domains from N- to C-terminus:
| Region or feature | Position in precursor | Structural or biochemical role | Evidence basis |
|---|---|---|---|
| Signal peptide | N terminus | Directs the nascent precursor into the secretory pathway; consistent with maturation through the ER and Golgi before delivery to membrane compartments. | Canonical ADAM10 architecture; SUP-17 is annotated as a precursor and localizes in the ER and at the cell surface (morbidelli2026inhibitionofadam10 pages 35-40, wang2018dissectingtherole pages 130-136) |
| Prodomain | After signal peptide, before catalytic domain | Assists folding as an intramolecular chaperone and maintains the zymogen in an inactive state. Its conserved cysteine ligates the catalytic Zn²⁺—the cysteine-switch mechanism—thereby blocking proteolysis before maturation. | Established ADAM10/ADAM-family mechanism inferred for the SUP-17 ortholog (wang2018dissectingtherole pages 22-28, seals2003theadamsfamily pages 4-5) |
| Metalloproteinase domain | Extracellular, N-terminal portion of mature enzyme | Catalyzes peptide-bond hydrolysis during ectodomain shedding. The conserved HExxHxxGxxH motif supplies three histidines that coordinate Zn²⁺; the glutamate activates water, generating a hydroxide nucleophile that attacks the substrate peptide bond. | Conserved active-ADAM catalytic mechanism and SUP-17 domain organization (wang2018dissectingtherole pages 22-28, seals2003theadamsfamily pages 4-5) |
| Disintegrin domain | Extracellular, C-terminal to catalytic domain | Contributes to the multidomain extracellular architecture and may help orient the catalytic region or mediate protein interactions; a SUP-17-specific binding partner or integrin interaction has not been established. | Domain assignment is supported, but its precise function in SUP-17 remains unresolved (morbidelli2026inhibitionofadam10 pages 35-40, wang2018dissectingtherole pages 22-28) |
| Cysteine-rich domain | Extracellular, after disintegrin domain | Likely contributes to substrate recognition, protein interactions, and positioning of the catalytic domain near membrane-proximal cleavage sites; this role is inferred from ADAM-family structure rather than directly demonstrated for SUP-17. | Conserved ADAM10 architecture (morbidelli2026inhibitionofadam10 pages 35-40, wang2018dissectingtherole pages 22-28) |
| EGF-like domain | Extracellular, proximal to membrane | Small extracellular module within the canonical ADAM architecture; may stabilize or space the ectodomain, but no SUP-17-specific biochemical function has been demonstrated. | Comparative ADAM10-family architecture (morbidelli2026inhibitionofadam10 pages 35-40, wang2018dissectingtherole pages 22-28) |
| Transmembrane domain | Single membrane-spanning segment | Anchors SUP-17 as a type I membrane protease, positioning its catalytic domain outside the cell or within the lumen of secretory/endosomal compartments. This topology supports cleavage of membrane-protein ectodomains. | ADAM10-family topology and observed SUP-17 plasma-membrane/endosomal localization (white2005theadamfamily pages 98-102, wang2018dissectingtherole pages 130-136, wang2018dissectingtherole pages 78-88) |
| Cytoplasmic tail | C terminus, intracellular | Potentially mediates trafficking, localization, and regulatory interactions; a specific signaling or trafficking motif has not been experimentally defined for SUP-17 in the cited studies. | Conserved domain architecture; function remains inferential (morbidelli2026inhibitionofadam10 pages 35-40, wang2018dissectingtherole pages 22-28) |
| Zymogen activation | Secretory pathway, principally during Golgi transit | SUP-17/ADAM10 is synthesized as an inactive precursor. Proprotein convertase cleavage removes the prodomain, disrupts the cysteine switch, and permits formation of the active Zn²⁺-dependent catalytic center. PC7 has been proposed for ADAM10, although the responsible convertase has not been directly established for worm SUP-17. | ADAM10-family maturation model applied to its C. elegans ortholog (white2005theadamfamily pages 98-102, saintpol2017regulationofthe pages 15-20, seals2003theadamsfamily pages 4-5) |
| Mature enzyme and reaction | Plasma membrane and intracellular membrane compartments | Functions as a membrane-associated zinc endopeptidase/sheddase (EC 3.4.24.81): substrate + H₂O → extracellular cleavage products. Cleavage releases an ectodomain and leaves a membrane-associated C-terminal fragment; in Notch signaling, this enables subsequent γ-secretase processing. | SUP-17/ADAM10 enzymatic classification and conserved shedding mechanism (saintpol2017regulationofthe pages 15-20, wang2018dissectingtherole pages 22-28, jarriault2005evidenceforfunctional pages 8-9) |
Table: Domain-by-domain summary of the SUP-17 precursor, its conserved zinc-metalloprotease mechanism, and activation by prodomain removal. The table distinguishes experimentally supported SUP-17 features from functions inferred through its orthology to ADAM10.
SUP-17 functions as a zinc-dependent endopeptidase that catalyzes the proteolytic cleavage of extracellular domains from membrane-bound proteins—a process known as ectodomain shedding (wang2018dissectingtherole pages 22-28, seals2003theadamsfamily pages 2-4). The catalytic mechanism involves:
The most well-characterized SUP-17 substrate identified through genetic evidence is UNC-40, the C. elegans homolog of mammalian neogenin/DCC (Deleted in Colorectal Cancer) (wang2018dissectingtherole pages 63-68, wang2017twoparalogoustetraspanins pages 11-13). Genetic experiments demonstrate that truncated UNC-40 proteins lacking the intracellular domain partially suppress sup-17 mutant phenotypes, while unc-40 null alleles do not, supporting a model in which SUP-17-dependent processing of UNC-40 promotes BMP signaling (wang2018dissectingtherole pages 63-68). However, the incomplete suppression indicates that additional, yet-unidentified substrates likely exist (wang2018dissectingtherole pages 63-68, wang2018dissectingtherole pages 130-136).
In the context of Notch signaling, SUP-17 participates in ligand-induced proteolytic processing of Notch receptors (LIN-12 and GLP-1), performing the S2 cleavage that exposes the receptor for subsequent γ-secretase processing and release of the Notch intracellular domain (saintpol2017regulationofthe pages 15-20, wang2018dissectingtherole pages 33-38, jarriault2005evidenceforfunctional pages 8-9).
One of the most extensively characterized roles of SUP-17 is in the bone morphogenetic protein (BMP) signaling pathway in C. elegans, known as the Sma/Mab pathway (wang2017twoparalogoustetraspanins pages 1-2, wang2017twoparalogoustetraspanins pages 8-11). This pathway regulates:
Genetic evidence demonstrates that SUP-17 functions within the Sma/Mab pathway rather than in a parallel pathway: sup-17 mutations do not enhance the small-body phenotypes of core BMP pathway mutants (dbl-1, sma-6, sma-3) but do suppress the M-lineage defects of sma-9 mutants (wang2018dissectingtherole pages 63-68, wang2018dissectingtherole pages 50-56).
Tissue-specific rescue experiments reveal that SUP-17 acts in signal-receiving cells: hypodermal expression rescues body-size defects, while M-lineage expression partially rescues mesodermal development phenotypes (wang2018dissectingtherole pages 63-68, wang2017twoparalogoustetraspanins pages 7-8, wang2017twoparalogoustetraspanins pages 8-11). This indicates that SUP-17 functions cell-autonomously in tissues that respond to BMP ligands rather than in signal-producing cells.
SUP-17 also participates in Notch signaling, where it functions as a Site 2 (S2) protease that cleaves Notch receptors after ligand binding (wang2018dissectingtherole pages 33-38, jarriault2005evidenceforfunctional pages 8-9, dunn2010aconservedtetraspanin pages 2-3). However, SUP-17 exhibits functional redundancy with ADM-4 (the C. elegans ADAM17/TACE ortholog) in this pathway (jarriault2005evidenceforfunctional pages 8-9, jarriault2005evidenceforfunctional pages 5-6).
Key findings regarding SUP-17 in Notch signaling include:
Importantly, while SUP-17 contributes to Notch signaling, it is not absolutely required—likely due to ADM-4 redundancy—and its requirement becomes evident primarily in sensitized genetic backgrounds or when both proteases are compromised (jarriault2005evidenceforfunctional pages 8-9, jarriault2005evidenceforfunctional pages 5-6).
SUP-17 exhibits a dynamic subcellular distribution pattern consistent with its role as a regulated membrane protease:
SUP-17 localizes to the cell surface, particularly enriched on basolateral rather than apical membranes in early embryos (wang2018dissectingtherole pages 130-136, wang2017twoparalogoustetraspanins pages 8-11). This cell-surface pool represents the functionally active form of the enzyme where it can access transmembrane substrates for ectodomain shedding (wang2017twoparalogoustetraspanins pages 8-11, wang2018dissectingtherole pages 38-43).
In addition to plasma membrane localization, SUP-17 is found in multiple intracellular membrane compartments:
Notably, SUP-17 is not detectably enriched in recycling endosomes marked by RAB-11 (wang2018dissectingtherole pages 78-88).
The subcellular distribution and trafficking of SUP-17 are regulated by TspanC8 family tetraspanins, particularly TSP-12 and TSP-14 (wang2017twoparalogoustetraspanins pages 1-2, wang2017twoparalogoustetraspanins pages 8-11):
Importantly, TSP-12 affects SUP-17 distribution rather than its overall abundance; total SUP-17 protein levels remain relatively constant in tetraspanin mutants (wang2018dissectingtherole pages 78-88, wang2018dissectingtherole pages 88-95).
SUP-17 is broadly expressed throughout C. elegans development from early embryogenesis through larval stages and adulthood (wang2017twoparalogoustetraspanins pages 8-11, wang2017twoparalogoustetraspanins pages 11-13). Specific expression domains identified using endogenously tagged SUP-17::GFP or reporter constructs include:
Endogenous neuronal expression was not definitively established in the cited studies, although tissue-specific rescue experiments tested neuronal promoters (wang2017twoparalogoustetraspanins pages 8-11, wang2017twoparalogoustetraspanins pages 7-8).
Strong loss-of-function or hypomorphic alleles such as sup-17(n1258) and sup-17(n316) are viable and display multiple developmental defects (wang2017twoparalogoustetraspanins pages 7-8, wang2018dissectingtherole pages 50-56):
Complete loss of SUP-17 function results in maternal-effect embryonic lethality, indicating an essential role in early development (wang2017twoparalogoustetraspanins pages 7-8, wang2018dissectingtherole pages 50-56, jarriault2005evidenceforfunctional pages 3-5, jarriault2005evidenceforfunctional pages 5-6). This lethality prevents analysis of null mutants in postembryonic developmental assays, and the viable alleles studied represent strong but non-null (hypomorphic) mutations (wang2017twoparalogoustetraspanins pages 7-8, wang2018dissectingtherole pages 50-56).
| Functional area | SUP-17 role or observation | Key evidence and interpretation |
|---|---|---|
| BMP/Sma/Mab signaling | Positively regulates BMP-pathway output in signal-receiving cells, contributing to normal body size, M-lineage development, and male-tail patterning. Loss of SUP-17 reduces RAD-SMAD reporter activity and genetically behaves within the Sma/Mab pathway rather than in a parallel growth pathway. (wang2018dissectingtherole pages 63-68, wang2017twoparalogoustetraspanins pages 11-13, wang2017twoparalogoustetraspanins pages 8-11) | Tissue-specific rescue supports cell-autonomous activity in recipient tissues: hypodermal expression rescues body size, while M-lineage expression partially rescues the mesodermal phenotype. Its BMP function is genetically separable from canonical Notch signaling. (wang2018dissectingtherole pages 63-68, wang2017twoparalogoustetraspanins pages 7-8) |
| Candidate BMP-pathway substrate | UNC-40, the C. elegans neogenin/DCC homolog and BMP modulator, is the strongest candidate SUP-17 substrate. Truncated UNC-40 proteins lacking the intracellular domain partially suppress sup-17 defects, whereas an unc-40 null allele does not. (wang2018dissectingtherole pages 63-68, wang2017twoparalogoustetraspanins pages 11-13) | These are genetic rather than direct biochemical cleavage data. They support a model in which SUP-17-dependent UNC-40 processing promotes BMP signaling, but the cleavage site and direct proteolysis remain unverified; incomplete suppression implies additional substrates. (wang2018dissectingtherole pages 63-68, wang2018dissectingtherole pages 130-136) |
| Notch/LIN-12 and GLP-1 signaling | Functions as an ADAM-family Site-2 protease that promotes Notch-receptor activation and cell-fate signaling. SUP-17 alone is not universally essential because the ADAM17-like protease ADM-4 supplies overlapping activity. (jarriault2005evidenceforfunctional pages 8-9, dunn2010aconservedtetraspanin pages 2-3, jarriault2005evidenceforfunctional pages 5-6) | Combined reduction of SUP-17 and ADM-4 causes reduced-Notch phenotypes, including two anchor cells instead of one, suppression of constitutively active GLP-1-associated germline proliferation, and sterility linked to spermathecal dysfunction. A constitutively active LIN-12 construct mimicking the post-Site-2 product suppresses much of the double-mutant sterility. (jarriault2005evidenceforfunctional pages 8-9, jarriault2005evidenceforfunctional pages 5-6) |
| Expression pattern | Broadly expressed from early embryogenesis through larval and adult stages. Endogenously tagged or reporter proteins were observed in embryos, hypodermis, M-lineage cells, intestinal precursor or intestinal cells, developing vulva, and adult gonad or germline-associated tissue. Endogenous neuronal expression was not established in the cited experiments. (wang2017twoparalogoustetraspanins pages 8-11, wang2017twoparalogoustetraspanins pages 11-13) | The broad pattern is consistent with roles in embryonic viability and multiple developmental pathways. Functional rescue specifically establishes relevant activity in hypodermal and M-lineage signal-receiving cells. (wang2017twoparalogoustetraspanins pages 8-11) |
| Mutant phenotypes | Viable strong loss-of-function or hypomorphic alleles cause reduced body size and severe male-tail abnormalities, including shortened or fused rays, a smaller fan, and crumpled spicules. They also partially suppress the sma-9 M-lineage defect. (wang2017twoparalogoustetraspanins pages 7-8, wang2018dissectingtherole pages 50-56, wang2017twoparalogoustetraspanins pages 8-11) | Complete loss produces maternal-effect embryonic lethality, indicating an essential early-developmental function. The temperature-sensitive allele also shows reduced male mating efficiency: 7/35 males produced cross-progeny at 20°C and 0/17 at 25°C in one study. (jarriault2005evidenceforfunctional pages 3-5, jarriault2005evidenceforfunctional pages 5-6, jarriault2005evidenceforfunctional pages 2-3) |
| Regulation by TSP-12 and TSP-14 | The TspanC8 tetraspanins TSP-12 and TSP-14 physically interact with SUP-17 and act redundantly with it to promote BMP- and Notch-related functions. TSP-12 has the clearest direct role in SUP-17 trafficking. (wang2017twoparalogoustetraspanins pages 1-2, dunn2010aconservedtetraspanin pages 2-3, wang2017twoparalogoustetraspanins pages 8-11) | Loss of TSP-12 reduces plasma-membrane SUP-17 and increases intracellular puncta or early/late-endosomal accumulation without a major reduction in total protein. TSP-14 binds SUP-17 but had little measurable effect on its localization in the tested embryonic assays, suggesting cell-type- or process-specific regulation. (wang2018dissectingtherole pages 130-136, wang2018dissectingtherole pages 78-88, wang2018dissectingtherole pages 88-95) |
Table: Summary of SUP-17 functions in BMP and Notch signaling, its expression and mutant phenotypes, and its regulation by TspanC8 tetraspanins. The table distinguishes direct observations from genetically inferred substrate relationships.
While SUP-17 itself has not been the primary focus of recent 2023-2024 publications, the broader Notch signaling pathway in C. elegans continues to be an active area of research:
Recent work by Murphy and colleagues (2023-2024) has revealed novel roles for the Notch signaling pathway in memory regulation through non-cell-autonomous mechanisms (murphy2024bodytobraininsulinand pages 1-4, zhou2023signalingfromthe pages 1-2). While these studies focus primarily on Notch ligands (OSM-11) and receptors (LIN-12) rather than SUP-17 specifically, they establish that:
Given SUP-17's established role as a Notch S2 protease (jarriault2005evidenceforfunctional pages 8-9, dunn2010aconservedtetraspanin pages 2-3), these findings suggest potential involvement of SUP-17 in non-autonomous regulation of cognitive function, though direct experimental evidence would be needed to confirm this.
A 2024 review by Lv et al. provides comprehensive analysis of Notch pathway evolution across invertebrates, confirming the high conservation of ADAM10/SUP-17 orthologs and their essential roles in Notch signaling from early-branching metazoans to bilaterians (lv2024evolutionandfunction pages 14-15). This evolutionary perspective reinforces the fundamental importance of ADAM10-family proteases in metazoan development.
Visual evidence from Wang et al. (2017) demonstrates the phenotypic consequences of sup-17 mutations (wang2017twoparalogoustetraspanins media 52ffe86e, wang2017twoparalogoustetraspanins media 73153288):
SUP-17/ADAM10 functions as a membrane-anchored zinc metalloprotease that regulates multiple developmental processes in C. elegans through controlled ectodomain shedding of transmembrane protein substrates. The protein operates at the intersection of at least two major signaling pathways:
BMP/Sma-Mab pathway: SUP-17 promotes BMP signaling by processing UNC-40/neogenin, thereby regulating body size, male tail development, and mesoderm formation. This function is genetically separable from Notch signaling and represents a novel role for ADAM10-family proteases (wang2018dissectingtherole pages 63-68, wang2017twoparalogoustetraspanins pages 1-2, wang2017twoparalogoustetraspanins pages 11-13).
Notch/LIN-12 pathway: SUP-17 acts redundantly with ADM-4 to perform S2 cleavage of Notch receptors, enabling cell-fate decisions in multiple developmental contexts including anchor cell specification and germline proliferation (jarriault2005evidenceforfunctional pages 8-9, jarriault2005evidenceforfunctional pages 5-6).
SUP-17 localizes to the plasma membrane (where it accesses substrates) and to intracellular compartments including the ER and endosomes (wang2018dissectingtherole pages 130-136, wang2018dissectingtherole pages 78-88). Its trafficking and cell-surface localization are regulated by TspanC8 tetraspanins TSP-12 and TSP-14, which bind SUP-17 and modulate its distribution without dramatically affecting total protein levels (wang2018dissectingtherole pages 130-136, wang2017twoparalogoustetraspanins pages 8-11, wang2018dissectingtherole pages 88-95).
The enzyme is essential for embryonic viability (null alleles are maternal-effect lethal), and hypomorphic alleles cause pleiotropic defects in growth, morphogenesis, and reproduction (wang2017twoparalogoustetraspanins pages 7-8, wang2018dissectingtherole pages 50-56, jarriault2005evidenceforfunctional pages 3-5). This essential nature reflects SUP-17's broad expression pattern and participation in multiple fundamental developmental pathways (wang2017twoparalogoustetraspanins pages 8-11, wang2017twoparalogoustetraspanins pages 11-13).
SUP-17/ADAM10 exemplifies the multifunctional nature of ADAM-family metalloproteases, participating in both classical (Notch) and non-canonical (BMP) signaling contexts through regulated proteolytic processing of membrane proteins. The C. elegans system has proven particularly valuable for dissecting these functions through genetic analysis, revealing substrate relationships and pathway interactions that may be conserved in other organisms. Future research directions include biochemical confirmation of direct SUP-17 cleavage sites on UNC-40 and other candidate substrates, investigation of potential roles in non-autonomous processes such as memory regulation, and further characterization of tetraspanin-mediated trafficking regulation.
Key Citations:
- Wang et al., 2017 (PLOS Genetics) - Identification of SUP-17 role in BMP signaling and tetraspanin regulation
- Wang, 2018 (PhD Thesis) - Comprehensive characterization of SUP-17 in BMP pathway
- Jarriault & Greenwald, 2005 (Developmental Biology) - Functional redundancy with ADM-4 in Notch signaling
- Liu et al., 2020 (PNAS) - Tetraspanin regulation of membrane protein trafficking
- Zhou et al., 2023 and Murphy et al., 2024 - Recent work on Notch signaling in memory regulation
References
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