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Biology subjects

Rubinstein, J.

Publications and source records attributed to Rubinstein, J..

2 recordsLinked to original sources

Anatomic set of mechanical models for the organ of Corti

We build a flexible platform for the study of the mechanical performance of the organ of Corti (OoC) in the transduction of basilar membrane (BM) vibrations to motion of an inner hair cell bundle (IHB). In this platform, each anatomic component of the OoC is described by an equation of motion that can be followed in time. We propose an initial set of models that attempt to capture the nonlinearities of somatic and bundle motility, but can nevertheless be easily handled. The anatomic components that we consider are the outer hair cells (OHCs), the outer hair cell bundles, Deiters cells, Hensen cells, the IHB and various sections of the reticular lamina. We study endolymph fluid motion in the subtectorial gap and then the mutual interactions among the components of the OoC, including the pressure exerted by endolymph. Minute bending of the apical ends of the OHCs can have a significant impact on the passage of motion from the BM to the IHB, including possible critical oscillator behaviour, even without the assistance of tectorial motion, shearing, or bundle motility. Thus, the components of the OoC could cooperate to enhance frequency selectivity, amplitude compression and signal to noise ratio in the passage from the BM to the IHB. Our models also provide a mechanism that could contribute to appropriate amplification of the wave travelling along the cochlea.

systems biology

Revised subunit order of mammalian septin complexes explains their in vitro polymerization properties

Septins are conserved GTP-binding cytoskeletal proteins that polymerize into filaments by end-to-end joining of heterooligomeric complexes. In human cells, both hexamers and octamers exist, and crystallography studies predicted the order of the hexamers to be SEPT7-SEPT6-SEPT2-SEPT2-SEPT6-SEPT7, while octamers are thought to have the same core, but with SEPT9 at the ends. However, based on this septin organization, octamers and hexamers would not be expected to co-polymerize due to incompatible ends. Here we isolated hexamers and octamers of specific composition from human cells and show that hexamers and octamers polymerize individually and, surprisingly, with each other. Binding of Borg3 results in distinctive clustering of each filament type. Moreover, we show that the organization of hexameric and octameric complexes is inverted compared to its original prediction. This revised septin organization is congruent with the organization and behavior of yeast septins suggesting that their properties are more conserved than was previously thought.

cell biology