The team led by John Hogenesch, PhD, a professor of Systems Pharmacology and Translational Therapeutics in the Perelman School of Medicine at University of Pennsylvania and Jason DeBruyne, PhD, a former postdoctoral fellow in the Hogenesch lab and now an assistant professor at Morehouse School of Medicine in Atlanta, applied their new method to identifying other clock partners that target a multipurpose
cell nucleus receptor for disposal.
Not exact matches
The red
cells are muscle
cells, the green areas are
receptors for neuronal input, and the blue patches are
cell nuclei.
These
receptors, called
receptor tyrosine kinases (RTKs), transmit instructions through the
cell wall and down through a cascade of reactions to a target gene in the
nucleus.
They work by binding to
receptors inside a
cell, which then travel to the
nucleus and act on the DNA by turning select genes on and off.
In addition, others (36) have shown that inhibition of exportin 1, a nuclear export
receptor, can lead to accumulation of p70S6K in the
nucleus of kidney
cells.
The researchers found that when they dosed
cells that expressed a2C - AR with chemicals that activate Rap1A, either directly or through means that involve another protein called Epac, the
cells drew from pools of a2C - AR near the
cell's
nucleus and moved these
receptors to the
cell surface.
Calcitriol mediates its biological effects by binding to the vitamin D
receptor (VDR), which is principally located in the
nuclei of target
cells.
The hormone enters the
cell, attached to a
receptor, and then enters the
nucleus of the
cell where it binds directly to the DNA.
Once this happens, the
receptor enters the
nucleus of its
cell and attaches to specific spots on the chromosomes that contain all of the
cell's genetic coding.