Structural instability in an autophosphorylating kinase switch.

نویسندگان

  • Michael Grinfeld
  • Steven D Webb
چکیده

We analyse a simple kinase model that exhibits bistability when there is no protein turnover, and show analytically that the property of being bistable is not necessarily conserved when degradation and synthesis of the kinase are taken into account.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

A mechanism for memory storage insensitive to molecular turnover: a bistable autophosphorylating kinase.

A mechanism is proposed for a molecular switch that can store information indefinitely, despite the complete turnover of the molecules that make up the switch. The design of the switch is based on known types of biochemical reactions. Central to the mechanism is a kinase that is activated by phosphorylation and capable of intermolecular autophosphorylation. It is shown that such a kinase and an...

متن کامل

Rat adrenocortical carcinoma 494 autophosphorylating protein kinase, autophosphorylating protein kinase 500. Purification, biochemical and immunological characterization, and substrate specificity.

A novel autophosphorylating protein kinase, autophosphorylating protein kinase 500, independent of cyclic AMP, cyclic GMP, calcium, and calmodulin was purified from rat adrenocortical carcinoma 494 by ammonium sulfate fractionation followed by the chromatographic steps of DEAE-cellulose, gel filtration, cyclic AMP-epoxy Sepharose, and phosphocellulose. Sometimes two additional chromatographic p...

متن کامل

The delicate bistability of CaMKII.

Calcium/calmodulin-dependent protein kinase II (CaMKII) is a synaptic, autophosphorylating kinase that is essential for learning and memory. Previous models have suggested that CaMKII functions as a bistable switch that could be the molecular correlate of long-term memory, but experiments have failed to validate these predictions. These models involved significant approximations to overcome the...

متن کامل

Differential sensitivity of the insulin-receptor kinase to thiol and oxidizing agents in the absence and presence of insulin.

The purified human placental insulin-receptor beta-subunit autophosphorylating activity was found to be inhibited, in a time- and concentration-dependent manner, by the specific thiol-alkylating agents N-ethylmaleimide and 5,5'-dithiobis-(2-nitrobenzoic acid). The insulin-receptor kinase was observed to be more sensitive to inhibition by N-ethylmaleimide in the presence [IC50 (concn, giving 50%...

متن کامل

A monoclonal antibody which identifies the autophosphorylation domain of autophosphorylating protein kinase 500.

Autophosphorylating protein kinase 500 is a serine protein kinase expressed progressively with the steps of cellular transformation, approaching levels from 50- to 100-fold in the terminal stages of malignancy. The enzyme possesses a sharply restricted range of substrates: itself and a ribosomal protein with a molecular weight of 31,000 (S6). We report here on the characterization of a monoclon...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Mathematical biosciences

دوره 219 2  شماره 

صفحات  -

تاریخ انتشار 2009