Intramolecular Conformational Changes Optimize Protein Kinase C Signaling
نویسندگان
چکیده
منابع مشابه
Intramolecular conformational changes optimize protein kinase C signaling.
Optimal tuning of enzyme signaling is critical for cellular homeostasis. We use fluorescence resonance energy transfer reporters in live cells to follow conformational transitions that tune the affinity of a multidomain signal transducer, protein kinase C (PKC), for optimal response to second messengers. This enzyme comprises two diacylglycerol sensors, the C1A and C1B domains, that have a suff...
متن کاملSignaling through protein kinase C.
Protein kinase C (PKC) comprises a large family of serine/threonine kinases which are activated by many extracellular signals. Inside the cell, PKCs are regulated by a variety of lipid second messengers, including the ubiquitous diacylglycerol and phosphatidylserine. Phosphorylation has also emerged as an important mechanism of regulation of all PKCs. Work in the last 20 years has provided evid...
متن کاملIntramolecular C2 Domain-Mediated Autoinhibition of Protein Kinase C βII.
The signaling output of protein kinase C (PKC) is exquisitely controlled, with its disruption resulting in pathophysiologies. Identifying the structural basis for autoinhibition is central to developing effective therapies for cancer, where PKC activity needs to be enhanced, or neurodegenerative diseases, where PKC activity should be inhibited. Here, we reinterpret a previously reported crystal...
متن کاملConformational changes underlying calcium/calmodulin-dependent protein kinase II activation.
Calcium/calmodulin-dependent protein kinase II (CaMKII) interprets information conveyed by the amplitude and frequency of calcium transients by a controlled transition from an autoinhibited basal intermediate to an autonomously active phosphorylated intermediate (De Koninck and Schulman, 1998). We used spin labelling and electron paramagnetic resonance spectroscopy to elucidate the structural a...
متن کاملIntramolecular Conformational Potentials
The previously developed theory for treating the kinematics of polymers in dense media (Bahar, I.; Erman, B.; Monnerie, L. Macromolecules 1992, 25, 6309, 6315) is extended to include the influence of internal conformational energy barriers on the mechanism of motion. The method is based on the solution of a constrained equation of motion in the presence of dissipative forces due to friction. Su...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Chemistry & Biology
سال: 2014
ISSN: 1074-5521
DOI: 10.1016/j.chembiol.2014.02.008