TY - JOUR
T1 - Dynamics of gradient formation by intracellular shuttling
AU - Berezhkovskii, Alexander M.
AU - Shvartsman, Stanislav Y.
N1 - Publisher Copyright:
© 2015 AIP Publishing LLC.
PY - 2015/8/21
Y1 - 2015/8/21
N2 - A number of important cellular functions rely on the formation of intracellular protein concentration gradients. Experimental studies discovered a number of mechanisms for the formation of such gradients. One of the mechanisms relies on the intracellular shuttling of a protein that interconverts between the two states with different diffusivities, under the action of two enzymes, one of which is localized to the plasma membrane, whereas the second is uniformly distributed in the cytoplasm. Recent work reported an analytical solution for the steady state gradient in this mechanism, obtained in the framework of a one-dimensional reaction-diffusion model. Here, we study the dynamics in this model and derive analytical expressions for the Laplace transforms of the time-dependent concentration profiles in terms of elementary transcendental functions. Inverting these transforms numerically, one can obtain time-dependent concentration profiles of the two forms of the protein.
AB - A number of important cellular functions rely on the formation of intracellular protein concentration gradients. Experimental studies discovered a number of mechanisms for the formation of such gradients. One of the mechanisms relies on the intracellular shuttling of a protein that interconverts between the two states with different diffusivities, under the action of two enzymes, one of which is localized to the plasma membrane, whereas the second is uniformly distributed in the cytoplasm. Recent work reported an analytical solution for the steady state gradient in this mechanism, obtained in the framework of a one-dimensional reaction-diffusion model. Here, we study the dynamics in this model and derive analytical expressions for the Laplace transforms of the time-dependent concentration profiles in terms of elementary transcendental functions. Inverting these transforms numerically, one can obtain time-dependent concentration profiles of the two forms of the protein.
UR - http://www.scopus.com/inward/record.url?scp=84939824975&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84939824975&partnerID=8YFLogxK
U2 - 10.1063/1.4928858
DO - 10.1063/1.4928858
M3 - Article
C2 - 26298124
AN - SCOPUS:84939824975
SN - 0021-9606
VL - 143
JO - Journal of Chemical Physics
JF - Journal of Chemical Physics
IS - 7
M1 - 074116
ER -