Abstract
While various approaches exist to study protein localization, it is still a challenge to predict where proteins localize. Here, we consider a mechanistic viewpoint for membrane localization. Taking into account the steps for the folding pathway of α-helical membrane proteins and relating biophysical parameters to each of these steps, we create a score capable of predicting the propensity for membrane localization and call it FP3mem. This score is driven from the principal component analysis (PCA) of the biophysical parameters related to membrane localization. FP3mem allows us to rationalize the colocalization of a number of channel proteins with the Cav1.2 channel by their fewer propensities for membrane localization.
Highlights
Calcium influx plays a significant role in controlling a variety of cellular functions, and is mainly carried out by voltage-gated Ca2+ channels [1,2]
L-type Ca2+ channels (LTCCs) channels consist of four isoforms: Cav1.1, Cav1.2, Cav1.3 and Cav1.4, of which Cav1.2 and Cav1.3 are more distributed and localize in diverse tissues [3,4,5,6,7,8,9,10,11]
We introduce the Folding Pathway-based Protein Propensity for membrane (FP3mem) score that is tightly associated with the tendency of proteins for being a-helical plasma membrane proteins
Summary
Calcium influx plays a significant role in controlling a variety of cellular functions, and is mainly carried out by voltage-gated Ca2+ channels [1,2]. Voltage-gated L-type Ca2+ channels (LTCCs) are involved in the regulation of muscle contraction, hormone secretion, neural excitability, gene expression and neurotransmitter release. Kohler et al cloned these channels in 1996 and found three subtypes: KCa2.1 (SK1), KCa2.2 (SK2) and KCa2.3 (SK3) [22]. These channels are voltage-independent but highly sensitive to [Ca2+]i due to the C- terminal bound calmodulin protein [16,23,24,25,26,27,28]. The channels are mainly located in the central and peripheral nervous systems [29,30,31,32,33]
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