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mec-2 encodes MEC-2, a stomatin-family membrane protein required for touch sensitivity in C. elegans. It binds cholesterol, associates with the MEC-4 and MEC-10 pore subunits, and raises the current the channel carries, acting together with MEC-6 to amplify it roughly two hundred fold.
It is an accessory factor rather than part of the conducting pore: single-molecule imaging finds the pore to be a MEC-4 : MEC-4 : MEC-10 trimer that does not stably associate with MEC-2. Loss leaves the neurons alive and correctly placed but unresponsive. CD BioSciences delivers custom mec-2 alleles — knockouts, domain mutants and tag knockins — with full genotype verification.
| Gene symbol | mec-2 (a stomatin-family membrane protein that binds cholesterol and scaffolds the degenerin channel, greatly increasing the current it carries) |
|---|---|
| Protein product | MEC-2 — stomatin-like cholesterol-binding scaffold of the touch receptor channel |
| Mammalian homolog | stomatin (STOM) and the wider SPFH / stomatin-prohibitin-flotillin family, including STOML1 to STOML3 and podocin (NPHS2); the central region of MEC-2 is about 65 percent identical to human stomatin |
| Biological role | MEC-2 is the linker that was proposed to connect the degenerin channel to the specialised microtubules inside the touch receptor neuron. It is a protein of 481 amino acids whose central region combines a short membrane-associated hydrophobic stretch with a cytoplasmic hydrophilic domain, and that central region is roughly 65 percent identical to human red blood cell stomatin; the C-terminus carries a proline-rich segment resembling an SH3-binding motif. Functionally it is a channel amplifier rather than a pore: co-expression with the MEC-4(d)/MEC-10(d) pair raises amiloride-sensitive sodium current substantially on its own and, together with MEC-6, by roughly two hundred fold, and MEC-2 interacts physically with MEC-4, MEC-10 and MEC-6. A caveat worth carrying into any design is that single-molecule imaging later failed to detect stable association of either MEC-2 or MEC-6 with the MEC-4 / MEC-10 trimer, so both proteins behave as accessory or maturation factors rather than as fixed core subunits. |
| Loss-of-function phenotype | Loss of mec-2 makes animals touch insensitive while leaving the six touch receptor neurons alive, correctly specified and correctly positioned, so this is a transduction defect rather than a fate or structural defect; the channel subunits are still expressed. Classical alleles such as mec-2(e75) are recessive, and the animals are otherwise healthy and coordinated. |
| Why edit it | It is the best-characterised stomatin-family protein in any genetically tractable animal, and the only one where the amplifying effect can be separated from channel expression inside a native, behaviourally scored circuit. Because stomatin-domain proteins are implicated in human channel regulation and in podocyte filtration, a validated mec-2 allelic series is a compact way to test whether cholesterol binding or scaffolding is what the domain actually contributes. It is also the historical bridge between the channel and the microtubule bundle, so it remains the first place to look when a candidate is thought to couple the two. |
| Recommended background | Standard N2 background. Behavioural scoring is sufficient for a null, but we recommend pairing any domain-separation allele with either in vivo recording or a current readout, because the interesting alleles change the size of the response rather than its presence, and a binary behavioural assay cannot resolve that. |
| Representative allele | The classical reference allele mec-2(e75) plus further alleles from the CGC collection; custom CRISPR nulls, separations of function that delete the proline-rich tail or disrupt the stomatin domain while leaving the membrane anchor intact, and epitope tag knockins. |
mec-2 at a glance: mec-2 loss makes touch neurons insensitive without killing them: the pore is made but carries far less current. Editing mec-2 alone is a powerful way to dissect MEC-2 function in vivo, with conserved relevance to human stomatin biology.
gRNA-guided Cas9 cutting with NHEJ repair to introduce frameshift indels, generating premature stop codons and null / strong-loss-of-function mec-2 alleles.
Homology-directed repair (HDR) inserts GFP / HA / FLAG or other tags at the mec-2 locus for endogenous expression and subcellular localization studies.
Introduce specific amino-acid substitutions to dissect functional domains and separate catalytic from scaffolding roles of MEC-2.
Build tissue-specific, inducible, or temperature-sensitive configurations and reporter lines for spatiotemporal analysis of MEC-2 function.
A straight null is uncomplicated here, but the more useful reagents are domain separations: removing the proline-rich C-terminus tests the proposed cytoskeletal coupling while leaving membrane association and the stomatin domain intact, and substitutions in the cholesterol-binding region test whether lipid interaction is the relevant activity. Do not assume a deletion reproduces a domain mutant — the two differ in degree rather than in kind — so quantify current or graded behaviour rather than scoring mere presence or absence.
Define target (knockout / knockin / point mutation), select gRNA(s) and HDR template, confirm against the latest genome build.
Design, validate, and synthesize high-specificity guide RNAs targeting the mec-2 locus.
Build Cas9 / gRNA delivery construct and, for knockin, the homology-arm repair template.
Perform gonadal microinjection of N2 animals with CRISPR components and co-CRISPR selection markers.
PCR, Sanger / sequencing, and phenotype confirmation to isolate edited animals and verify alleles.
Provide homozygous / balanced mec-2 strains plus a full genotype and methods report.
Standard knockout projects deliver a frameshift indel allele predicted to produce a premature stop and a loss-of-function phenotype. We confirm the edit by sequencing and, where relevant, by characteristic phenotype assays.
Yes. Using HDR with a designed repair template, we can insert GFP, HA, or FLAG tags at the C- or N-terminus while preserving endogenous promoter and regulation.
Timelines vary with editing type and validation needs, but our optimized pipeline and co-CRISPR selection typically shorten turnaround versus conventional approaches. Contact us with your design for a project-specific estimate.
The evidence supports regulator, with a historical caveat worth knowing. The work that cloned mec-6 described MEC-2 and MEC-6 together as channel-associated proteins that raise current dramatically, and MEC-2 was long modelled as a linker between the pore and the microtubules. Single-molecule imaging in Xenopus oocytes later showed that MEC-4 forms homotrimers and that MEC-4 with MEC-10 forms heterotrimers of defined stoichiometry, while MEC-2 and MEC-6 neither associate tightly with those trimers nor alter their stoichiometry. The consistent reading is that the pore is a MEC-4 : MEC-4 : MEC-10 trimer and that MEC-2 and MEC-6 act on it, through maturation, trafficking or the local membrane environment, rather than sitting in it. In the animal the distinction shows up as a requirement for punctate channel localisation rather than as a change in channel composition.
CD BioSciences is committed to convenient, efficient, and cost-effective C. elegans model customization. Tell us your target design — knockout, knockin, tagging, or point mutation — and our scientists will respond with a tailored plan and quote.
Contact UsReferences
1. Kim H. M., Colaiácovo M. P. CRISPR-Cas9-guided genome engineering in C. elegans. Current Protocols in Molecular Biology, 2016, 115(1): 31.7.1–31.7.18.
2. Huang M., Gu G., Ferguson E. L., Chalfie M. A stomatin-like protein necessary for mechanosensation in C. elegans. Nature, 1995, 378(6554): 292–295.
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