Hall helps Ohm: some corrections to negative-U centers approach to transport properties of YBa2_2Cu3_3Ox_x and La2−x_{2-x}Srx_xCuO4_4

For broad oxygen and strontium doping ranges, temperature dependences (T-dependences) of the normal state resistivity \rho(T) of YBa_2Cu_3O_x (YBCO) and La_(2-x)Sr_xCuO_4 (LSCO) are calculated and compared to experiments. Holes transport was taken in the \tau-approximation, where \tau(T,\epsilon) is due to acoustic phonons. Besides, T-dependence of the chemical potential \mu(T) and effective carrier mass m* ~10-100 free electron masses, obtained by negative-U centers modelling the T-dependence of the Hall coefficient, were used to calculate \rho(T). In addition, it is demonstrated that anisotropy of the cuprates does not affect the calculated T-variation of neither Hall coefficient nor \rho, but only rescale their magnitudes by factors depending on combinations of m_ab and m_c.Comment: 4th International Conference Fundamental Problems of High-Temperature Superconductivity, Moscow-Zvenigorod (October 3-7, 2011) Submitted to J. Supercond. Nov. Magn.: after revision. Extension for Supercond. Sci. Technol. 24 075026 (2011), DOI: 10.1088/0953-2048/24/7/075026 Contains: 2 pages, 3 figure

Symmetry breaking in the female germline cyst.

In mammals and flies, only one cell in a multicellular female germline cyst becomes an oocyte, but how symmetry is broken to select the oocyte is unknown. Here, we show that the microtubule (MT) minus end-stabilizing protein Patronin/CAMSAP marks the future Drosophila oocyte and is required for oocyte specification. The spectraplakin Shot recruits Patronin to the fusome, a branched structure extending into all cyst cells. Patronin stabilizes more MTs in the cell with the most fusome material. Our data suggest that this weak asymmetry is amplified by Dynein-dependent transport of Patronin-stabilized MTs. This forms a polarized MT network, along which Dynein transports oocyte determinants into the presumptive oocyte. Thus, Patronin amplifies a weak fusome anisotropy to break symmetry and select one cell to become the oocyte

Periodic actin structures in neuronal axons are required to maintain microtubules

Axons are the cable-like neuronal processes wiring the nervous system. They contain parallel bundles of microtubules as structural backbones, surrounded by regularly-spaced actin rings termed the periodic membrane skeleton (PMS). Despite being an evolutionarily-conserved, ubiquitous, highly-ordered feature of axons, the function of PMS is unknown. Here we studied PMS abundance, organisation and function, combining versatile Drosophila genetics with super-resolution microscopy and various functional readouts. Analyses with 11 different actin regulators and 3 actin-targeting drugs suggest PMS to contain short actin filaments which are depolymerisation resistant and sensitive to spectrin, adducin and nucleator deficiency - consistent with microscopy-derived models proposing PMS as specialised cortical actin. Upon actin removal we observed gaps in microtubule bundles, reduced microtubule polymerisation and reduced axon numbers suggesting a role of PMS in microtubule organisation. These effects become strongly enhanced when carried out in neurons lacking the microtubule-stabilising protein Short stop (Shot). Combining the aforementioned actin manipulations with Shot deficiency revealed a close correlation between PMS abundance and microtubule regulation, consistent with a model in which PMS-dependent microtubule polymerisation contributes to their maintenance in axons. We discuss potential implications of this novel PMS function along axon shafts for axon maintenance and regeneration

The Shot CH1 domain recognises a distinct form of F-actin during<i>Drosophila</i>oocyte determination

AbstractAs in mammals, only one cell in aDrosophilamulticellular female germline cyst is specified as an oocyte. The symmetry-breaking cue for oocyte selection is provided by the fusome, a tubular structure connecting all cells in the cyst. TheDrosophilaspectraplakin Shot localises to the fusome and translates its asymmetry into a polarised microtubule network that is essential for oocyte specification, but how Shot recognises the fusome is unclear. Here we demonstrate that Shot’s actin-binding domain (ABD) is necessary and sufficient to localise Shot to the fusome and mediates Shot function in oocyte specification together with the microtubule-binding domains. The calponin homology domain 1 of Shot’s ABD recognises fusomal F-actin and distinguishes it from other forms of F-actin in the cyst. By contrast, the ABDs of Utrophin, Fimbrin, Filamin, as well as Lifeact and F-tractin do not recognise fusomal F-actin. We therefore propose that Shot propagates fusome asymmetry by recognising a specific conformational state of F-actin on the fusome.</jats:p

Symmetry breaking in the female germline cyst

Specifying one oocyte from many In many animals, only one cell from a cyst of germ cells is selected to become the oocyte. Using fruit flies as a model, Nashchekin et al . identified the microtubule minus end-binding protein Patronin/CAMSAP as a key factor for specifying oocyte fate. Patronin amplifies an initial asymmetry provided by the fusome to form a noncentrosomal microtubule network focused on one cell, along which dynein transports oocyte fate determinants. This mechanism for selecting a single oocyte may be shared in other organisms. —BAP </jats:p

Symmetry breaking in the female germline cyst

AbstractIn mammals and flies, only a limited number of cells in a multicellular female germline cyst become oocytes, but how the oocyte is selected is unknown. Here we show that the microtubule minus end-stabilizing protein, Patronin/CAMSAP marks the future Drosophila oocyte and is required for oocyte specification. The spectraplakin, Shot, recruits Patronin to the fusome, a branched structure extending into all cyst cells. Patronin stabilizes more microtubules in the cell with most fusome and this weak asymmetry is amplified by Dynein-dependent transport of Patronin-stabilized microtubules. This forms a polarized microtubule network, along which Dynein transports oocyte determinants into the presumptive oocyte. Thus, Patronin amplifies a weak fusome anisotropy to break cyst symmetry. These findings reveal a molecular mechanism of oocyte selection in the germline cyst.</jats:p