A dynamin-related protein required for nuclear remodeling in Tetrahymena.
Dynamin-related proteins (DRPs) are GTPases that reversibly assemble on cellular membranes [1]. Individual DRPs (here "DRP" includes authentic dynamins) function in fission or tubulation of the plasma membrane, trans-Golgi network, mitochondria, peroxisomes, chloroplasts, and endosomes [1] and in mitochondrial fusion [2]. Many of these functions are widespread; they are present in animals, plants, trypanosomes, Giardia, ciliates, alga, and slime molds [3-8]. Lineage-specific expansions of the gene family created specialized DRPs. In animals, such DRPs include MxB, which has been reported to regulate nuclear-pore transport [9]. Whereas many unicellular organisms possess a small number of DRPs, expansions occurred in some protist lineages. The eight DRPs in the ciliate Tetrahymena thermophila might contribute to aspects of ciliate complexity. Each ciliate cell contains distinct germline and somatic nuclei, whose differentiation and maintenance must require distinct machinery [10, 11]. Here we show that Drp6p, previously shown to be targeted to the nuclear envelope [3], is required for macronuclear development. Drp6p activity, which is distinct from that of the only other known nuclear DRP, is modulated by a combination of stage-specific subcellular targeting and assembly dynamics. This work demonstrates a novel DRP activity and presents a system in which environmental and developmental cues can be used for manipulating key aspects of regulation.
Rahaman
Abdur
A
Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637, USA.
Elde
Nels C
NC
Turkewitz
Aaron P
AP
D000818:Animals; D053144:Cell Nucleus Shape; D053145:Cell Nucleus Size; D003227:Conjugation, Genetic; D019143:Evolution, Molecular; D020558:GTP Phosphohydrolases / Q000235:genetics / Q000378:metabolism*; D005810:Multigene Family; D013217:Starvation; D016808:Tetrahymena thermophila / Q000166:cytology* / Q000502:physiology
D020558:GTP Phosphohydrolases