期刊
JOURNAL OF CELL SCIENCE
卷 124, 期 21, 页码 3619-3630出版社
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.085159
关键词
Sarcoplasmic reticulum; Skeletal muscle; Ankyrin
类别
资金
- National Institutes of Health [F32 AR52768, F32 AR057647, RO1 AR52768, RO1 HL64304, RO1 AR56330]
- Muscular Dystrophy Association
Small ankyrin 1 (sAnk1; Ank1.5) is a similar to 20 kDa protein of striated muscle that concentrates in the network compartment of the sarcoplasmic reticulum (nSR). We used siRNA targeted to sAnk1 to assess its role in organizing the sarcoplasmic reticulum (SR) of skeletal myofibers in vitro. siRNA reduced sAnk1 mRNA and protein levels and disrupted the organization of the remaining sAnk1. Sarcomeric proteins were unchanged, but two other proteins of the nSR, SERCA and sarcolipin, decreased significantly in amount and segregated into distinct structures containing sarcolipin and sAnk1, and SERCA, respectively. Exogenous sAnk1 restored SERCA to its normal distribution. Ryanodine receptors and calsequestrin in the junctional SR, and L-type Ca2+ channels in the transverse tubules were not reduced, although their striated organization was mildly altered. Consistent with the loss of SERCA, uptake and release of Ca2+ were significantly inhibited. Our results show that sAnk1 stabilizes the nSR and that its absence causes the nSR to fragment into distinct membrane compartments.
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