6gzc
heterotetrameric katanin p60:p80 complex
Structural highlights
Function[KTNB1_MOUSE] Participates in a complex which severs microtubules in an ATP-dependent manner. May act to target the enzymatic subunit of this complex to sites of action such as the centrosome. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth.[HAMAP-Rule:MF_03022] [KTNA1_MOUSE] Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth (By similarity).[HAMAP-Rule:MF_03023] Publication Abstract from PubMedKatanin is a microtubule-severing enzyme that is crucial for many cellular processes. Katanin consists of two subunits, p60 and p80, that form a stable complex. The interaction between subunits is mediated by the p60 N-terminal microtubule-interacting and -trafficking domain (p60-MIT) and the p80 C-terminal domain (p80-CTD). Here, we performed a biophysical characterization of the mouse p60-MIT:p80-CTD heterodimer and show that this complex can assemble into heterotetramers. We identified two mutations that enhance heterotetramer formation and determined the X-ray crystal structure of this mutant complex. The structure revealed a domain-swapped heterotetramer consisting of two p60-MIT:p80-CTD heterodimers. Structure-based sequence alignments suggest that heterotetramerization of katanin might be a common feature of various species. Furthermore, we show that enhanced heterotetramerization of katanin impairs its microtubule end-binding properties and increases the enzyme's microtubule lattice binding and severing activities. Therefore, our findings suggest the existence of different katanin oligomers that possess distinct functional properties. Crystal Structure of a Heterotetrameric Katanin p60:p80 Complex.,Faltova L, Jiang K, Frey D, Wu Y, Capitani G, Prota AE, Akhmanova A, Steinmetz MO, Kammerer RA Structure. 2019 Jul 24. pii: S0969-2126(19)30234-5. doi:, 10.1016/j.str.2019.07.002. PMID:31353241[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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