TorsinA Neuron Volume 31, Issue 1, Pages 9-12 (July 2001)

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TorsinA Neuron Volume 31, Issue 1, Pages 9-12 (July 2001) Xandra O. Breakefield, Christoph Kamm, Phyllis I. Hanson Neuron Volume 31, Issue 1, Pages 9-12 (July 2001) DOI: 10.1016/S0896-6273(01)00350-6

Figure 1 Phylogenetic Relationships among Torsins and Related Proteins Torsins and torsin-related proteins (torps) revealed by cloning and database searches are shown in an unrooted tree with the length of connecting lines indicating their evolutionary distance. The current nomenclature is modified from Ozelius et al. (1999). (HSP104 and HSP101 are Clp/Hsp100 proteins.) Neuron 2001 31, 9-12DOI: (10.1016/S0896-6273(01)00350-6)

Figure 2 Early Embryogenesis in C. elegans Anterior is to the left. (A) Both the AB and the P1 cells inherit a centrosome that duplicates, and the daughter centrosomes (open circles) migrate (arrows) to opposite sides of the nucleus (solid circles). (B) In the P1 cell, the centrosome-nuclear complex undergoes a 90° rotation (arrows) oriented toward an anterior cortical site (gray oval). (C) This results in alignment of the P1 spindle along the anterior-posterior axis of the embryo. (Modified from Basham and Rose, 1999.) Neuron 2001 31, 9-12DOI: (10.1016/S0896-6273(01)00350-6)

Figure 3 Hypothetical Models of Dominant Effects of GAG-Deleted TorsinA TorsinA monomers (gray balls) are predicted to from a six-membered doughnut-like ring structure within the lumen of the ER. Monomers may be tethered to the ER membrane via hydrophobic sequences in the N terminus (Ozelius et al., 1997). The loss of the glutamic acid residue (red dot) in the C-terminal (blue line) of one or more subunits might act to disrupt closure of the ring (top) or interaction with a partner protein (pink balls; bottom) Neuron 2001 31, 9-12DOI: (10.1016/S0896-6273(01)00350-6)