6lag
Solution structure of SPA-2 SHDSolution structure of SPA-2 SHD
Structural highlights
FunctionPublication Abstract from PubMedThe Spitzenkorper (SPK) constitutes a collection of secretory vesicles and polarity-related proteins intimately associated with polarized growth of fungal hyphae. Many SPK-localized proteins are known, but their assembly and dynamics remain poorly understood. Here, we identify protein-protein interaction cascades leading to assembly of two SPK scaffolds and recruitment of diverse effectors in Neurospora crassa. Both scaffolds are transported to the SPK by the myosin V motor (MYO-5), with the coiled-coil protein SPZ-1 acting as cargo adaptor. Neither scaffold appears to be required for accumulation of SPK secretory vesicles. One scaffold consists of Leashin-2 (LAH-2), which is required for SPK localization of the signalling kinase COT-1 and the glycolysis enzyme GPI-1. The other scaffold comprises a complex of Janus-1 (JNS-1) and the polarisome protein SPA-2. Via its Spa homology domain (SHD), SPA-2 recruits a calponin domain-containing F-actin effector (CCP-1). The SHD NMR structure reveals a conserved surface groove required for effector binding. Similarities between SPA-2/JNS-1 and the metazoan GIT/PIX complex identify foundational features of the cell polarity apparatus that predate the fungal-metazoan divergence. Spitzenkorper assembly mechanisms reveal conserved features of fungal and metazoan polarity scaffolds.,Zheng P, Nguyen TA, Wong JY, Lee M, Nguyen TA, Fan JS, Yang D, Jedd G Nat Commun. 2020 Jun 5;11(1):2830. doi: 10.1038/s41467-020-16712-9. PMID:32503980[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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