Worcester Foundation for Biomedical Research

About: Worcester Foundation for Biomedical Research is a based out in . It is known for research contribution in the topics: Estrone & Estrogen. The organization has 2195 authors who have published 2646 publications receiving 115809 citations. The organization is also known as: Worcester Foundation for Experimental Biology.

Isolation and Characterization of New Fission Yeast Cytokinesis Mutants

Abstract: Schizosaccharomyces pombe is an excellent organism in which to study cytokinesis as it divides by medial fission using an F-actin contractile ring. To enhance our understanding of the cell division process, a large genetic screen was carried out in which 17 genetic loci essential for cytokinesis were identified, 5 of which are novel. Mutants identifying three genes, rng3(+), rng4(+), and rng5(+), were defective in organizing an actin contractile ring. Four mutants defective in septum deposition, septum initiation defective (sid)1, sid2, sid3, and sid4, were also identified and characterized. Genetic analyses revealed that the sid mutants display strong negative interactions with the previously described septation mutants cdc7-24, cdc11-123, and cdc14-118. The rng5(+), sid2(+), and sid3(+) genes were cloned and shown to encode Myo2p (a myosin heavy chain), a protein kinase related to budding yeast Dbf2p, and Spg1p, a GTP binding protein that is a member of the ras superfamily of GTPases, respectively. The ability of Spg1p to promote septum formation from any point in the cell cycle depends on the activity of Sid4p. In addition, we have characterized a phenotype that has not been described previously in cytokinesis mutants, namely the failure to reorganize actin patches to the medial region of the cell in preparation for septum formation.

Review: the use of isotopic steroids for the measurement of production rates in vivo.

Abstract: The most obvious purpose of the use of isotopic steroids to obtain secretion rates in vivohas been to minimize the disturbance caused by the observation to the prevailing secretion rate. This is more likely to occur when direct methods of analysis involving collection of venous blood from the gland are employed.

Microtubule-associated protein 1C from brain is a two-headed cytosolic dynein

Abstract: Dynein, an ATPase, is the force-generating protein in cilia and flagella1. It has long been speculated that cytoplasmic microtubules contain a related enzyme involved in cell division2 or in intracellular organelle transport3. A 'cytoplasmic dynein' has been described in sea urchin eggs4,5, but because the egg stockpiles precursors for both cytoplasmic and ciliary microtubules, the role of this enzyme in the cell has remained unresolved. We recently found that the microtubule-associated protein (MAP) 1C (ref. 6) from brain is a microtubule-activated ATPase7 that produces force in the direction corresponding to retrograde organelle transport in the cell8. MAP 1C has several similar properties to ciliary and flagellar dynein7–9. Here we show directly, using scanning transmission electron microscopy, that MAP 1C is structurally equivalent to the ciliary and flagellar enzyme and is the long-sought cytoplasmic analogue of this enzyme.