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1 Cell Biology and Biochemistry, Pacific Northwest National Laboratory, Richland, Washington, United States
2 Biological Sciences, PNNL/Battelle, Richland , Washington, United States
3 Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, Illinois, United States
4 Cell Biology and Biochemistry, Pacific Northwest National Laboratory, Richalnd, Washington, United States; Washington State University
5 Cell Biology and Biochemistry, Pacific Northwest National Laboratory, U. of Kansas, Richland, Washington, United States; Cell Biology and Biochemistry, Pacific Northwest National Laboratory, Richalnd, Washington, United States; Department of Biochemistry, Pacific Northwest National Laboratory, U. of Kansas, Haworth Hall, Lawrence, 66045-2106, United States
* To whom correspondence should be addressed. E-mail: diana.bigelow{at}pnl.gov.
Phospholamban (PLB) associates with the Ca-ATPase in sarcoplasmic reticulum (SR) membranes to permit the modulation of contraction in response to beta-adrenergic signaling. To understand how coordinated changes in the abundance and intracellular trafficking of PLB and the Ca-ATPase contribute to the maturation of functional muscle, we have measured changes in abundance, location, and turnover of endogenous and tagged proteins in myoblasts and during their differentiation. We find that PLB is constitutively expressed in both myoblasts and differentiated myotubes, whereas abundance increases of the Ca-ATPase coincide with the formation of differentiated myotubes. We observe that PLB is primarily present in highly mobile vesicular structures outside the endoplasmic reticulum, irrespective of the expression of the Ca-ATPase, indicating that PLB targeting is regulated through vesicle trafficking. Moreover, using pulse chase methods, we observe that in myoblasts PLB is trafficked through directed transport through the Golgi to the plasma membrane prior to endosome-mediated internalization. The observed trafficking of PLB to the plasma membrane suggests an important role for PLB during muscle differentiation, which is distinct from its previously recognized role in the regulation of the Ca-ATPase.
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