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Fig. 6 | Neural Development

Fig. 6

From: The model of local axon homeostasis - explaining the role and regulation of microtubule bundles in axon maintenance and pathology

Fig. 6

A molecular perspective of microtubule properties. a Cross-section of a MT with 14 protofilaments (PF) and lateral view of a 13 PF MT, both in B-lattice configuration, where α-tubulins make lateral bonds with α-tubulins and ß with ß, except at the seam (magenta line: seam; dashed red line: PF). b Close-up of an α/ß-tubulin heterodimer showing the various post-translational modification sites as indicated; note that the GTP of ß-tubulin in lattices is usually hydrolysed (GDP). c A 13 PF MT (top), cut open at the seam and rolled out (bottom); the yellow line shows the diameter, the white line follows the helical rise of laterally bonded tubulins; in 13 PF MTs, tubulins are precisely aligned at the seam (yellow arrow head) but shifted by three positions (3-start helix). d When deviating from the 13 PF prototype, tubulins are misaligned at the seam (orange arrow head); when forced into alignment, the PFs skew (deviation of the magenta line from the white stippled line), causing a super-twist of the MT as described by the 'lattice accommodation model' [98, 412]; for certain PF numbers, MTs can form two alternative alignments, of which usually the version with the lower helix start value (left) has a left-handed super-twist, whereas the higher value is right-handed [98]. e MTs behave like rigid rods with a persistence length of up to 10 mm, but can be bent down to diameters of curvature of ~1μm before they break; it has been reported that their cross-sectional profile may flatten above a certain threshold (black arrow head), thus softening the tube. f Lattices of GDP-tubulin are 1-3% shorter than MTs that were polymerised with the non-hydrolysable GTP analogue GMPCPP, or stabilised with taxol (orange structure binding α-tubulin in a 1:1 ratio, according to [413]); binding of kinesin-1 causes similar lengthening of tubulin (and additional compactions in the tubulin structure: yellow stars) which may cause cooperative binding of further kinesins and induce curvature if occurring only on one side of the MT; in extended taxol-bound MTs, bending forces were suggested to change tubulins on the concave side into their short conformation as an energetically favoured condition. For further references see main text

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