High impact information on Mtor

• The TPR snap helix: a novel protein repeat motif from mitosis to transcription [1].
• However, during mitosis Megator reorganizes and aligns together with Skeletor and Chromator into a fusiform spindle structure [2].
• During interphase Megator is localized to the nuclear rim and occupies the intranuclear space surrounding the chromosomes [2].
• On the basis of these findings we propose that the COOH-terminal domain of Megator functions as a targeting and localization domain, whereas the NH2-terminal domain is responsible for forming polymers that may serve as a structural basis for the putative spindle matrix complex [2].
• The Megator metaphase spindle persists in the absence of microtubule spindles, strongly implying that the existence of the Megator-defined spindle does not require polymerized microtubules [2].

Biological context of Mtor

• Megator, an essential coiled-coil protein that localizes to the putative spindle matrix during mitosis in Drosophila [2].
• The localization of coiled-coil Bx34 to both the nuclear interior and nuclear pore complexes and its sequence similarity to a known nuclear pore complex protein leads to speculations about a role for Bx34 in nucleo-cytoplasmic transport which we can test using molecular genetic approaches [3].
• The unusual crn protein consists of sixteen tandem repeats of the 34 amino acid tetratricopeptide (TPR) protein recognition domain [4].
• EAST and Megator also colocalize to the intranuclear space surrounding the chromosomes at interphase [5].
• The Drosophila crooked neck (crn) gene encodes an unusual TPR-containing protein whose function is essential for embryonic development [6].

Anatomical context of Mtor

• In the nuclear periphery, Bx34 localizes on or near nuclear pore complexes [3].
• Biochemically, Bx34 isolates exclusively with the nuclear matrix fraction [3].

Associations of Mtor with chemical compounds

• Control of triglyceride storage by a WD40/TPR-domain protein [7].

Other interactions of Mtor

• We have used immunocytochemistry to demonstrate that the EAST protein in Drosophila, which forms an expandable nuclear endoskeleton at interphase, redistributes during mitosis to colocalize with the spindle matrix proteins, Megator and Skeletor [5].

Analytical, diagnostic and therapeutic context of Mtor

• However, we show by immunoprecipitation experiments that EAST is likely to molecularly interact with Megator which has a large NH2-terminal coiled-coil domain with the capacity for self assembly [5].
• This is supported by the fact that in yeast two hybrid assays the tetratricopeptide repeat E (TPR E) of Rols7 shows interaction with the intracellular domain of Duf/Kirre [8].

References