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Expression of human tau inCaenorhabditis elegansneurons causes accumulation of aggregated tau leading to neurodegeneration and uncoordinated movement. We used this model of human tauopathy disorders to screen for genes required for tau neurotoxicity. Recessive loss-of-function mutations in thesut-2locus suppress the Unc phenotype, tau aggregation and neurodegenerative changes caused by human tau. We cloned thesut-2gene and found it encodes a novel sub-type of CCCH zinc finger protein conserved across animal phyla. SUT-2 shares significant identity with the mammalian SUT-2 (MSUT-2). To identify SUT-2 interacting proteins, we conducted a yeast two hybrid screen and found SUT-2 binds to ZYG-12, the soleC.elegansHOOK protein family member. Likewise, SUT-2 binds ZYG-12 inin vitroprotein binding assays. Furthermore, loss of ZYG-12 leads to a marked upregulation of SUT-2 protein supporting the connection between SUT-2 and ZYG-12. The human genome encodes three homologs of ZYG-12: HOOK1, HOOK2 and HOOK3. Of these, the human ortholog of SUT-2 (MSUT-2) binds only to HOOK2 suggesting the interaction between SUT-2 and HOOK family proteins is conserved across animal phyla. The identification ofsut-2as a gene required for tau neurotoxicity inC.elegansmay suggest new neuroprotective strategies capable of arresting tau pathogenesis in tauopathy disorders.

SUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegans