Small, Membrane-bound, Alternatively Spliced Forms of Ankyrin 1 Associated with the Sarcoplasmic Reticulum of Mammalian Skeletal Muscle

Zhou, Daixing; Birkenmeier, Connie S.; Williams, McRae W.; Sharp, John J.; Barker, Jane E.; Bloch, Robert J.

doi:10.1083/jcb.136.3.621

Cited by 89 publications

(109 citation statements)

References 61 publications

(91 reference statements)

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“…For example, the organization of small ankyrin 1 in the sarcoplasmic reticulum around Zdisks and M-lines (Zhou et al, 1997) remained largely unchanged in myofibers expressing exogenous K19 (Figures 7, M-O, and 8). Perhaps more remarkably, the distribution of ␤-dystroglycan between the sarcolemma and the myoplasm was also unaffected by overexpression of K19 ( Figures 7R and 8).…”

Section: Overexpression Of K8 and K19 In Muscle Fibersmentioning

confidence: 99%

Specific Interaction of the Actin-binding Domain of Dystrophin with Intermediate Filaments Containing Keratin 19

Stone

O’Neill

Catino

et al. 2005

MBoC

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Cytokeratins 8 and 19 concentrate at costameres of striated muscle and copurify with the dystrophin-glycoprotein complex, perhaps through the interaction of the cytokeratins with the actin-binding domain of dystrophin. We overexpressed dystrophin's actin-binding domain (Dys-ABD), K8 and K19, as well as closely related proteins, in COS-7 cells to assess the basis and specificity of their interaction. Dys-ABD alone associated with actin microfilaments. Expressed with K8 and K19, which form filaments, Dys-ABD associated preferentially with the cytokeratins. This interaction was specific, as the homologous ABD of ␤I-spectrin failed to interact with K8/K19 filaments, and Dys-ABD did not associate with desmin or K8/K18 filaments. Studies in COS-7 cells and in vitro showed that Dys-ABD binds directly and specifically to K19. Expressed in muscle fibers in vivo, K19 accumulated in the myoplasm in structures that contained dystrophin and spectrin and disrupted the organization of the sarcolemma. K8 incorporated into sarcomeres, with no effect on the sarcolemma. Our results show that dystrophin interacts through its ABD with K19 specifically and are consistent with the idea that cytokeratins associate with dystrophin at the sarcolemma of striated muscle. INTRODUCTIONMutations in the gene for dystrophin cause Duchenne or Becker Muscular Dystrophy, but we still know little about dystrophin's functions in normal muscle or how its absence leads to the loss of myofibers. Dystrophin is the major cytoskeletal component of a large, transmembrane complex (Ahn and Kunkel, 1993;Matsumura and Campbell, 1994;Ozawa et al., 1998) that plays a role in signaling from the plasma membrane of skeletal myofibers (sarcolemma) to the cytoplasm (Rando, 2001;Lapidos et al., 2004) and in transmitting the force of contraction across the sarcolemma to extracellular structures (Campbell, 1995;Bloch and Gonzalez-Serratos, 2003). Here, we focus on the latter role, and particularly, on the nature of the connections made between the contractile apparatus and the sarcolemma, at sites termed "costameres" (Bloch and Gonzalez-Serratos, 2003;Ervasti, 2003).Costameres are riblike structures that surround each myofiber at the sarcolemma and that are enriched in a number of integral and peripheral membrane proteins (Bloch and Gonzalez-Serratos, 2003;Ervasti, 2003), including dystrophin (Masuda et al., 1992;Minetti et al., 1992;Porter et al., 1992;Straub et al., 1992;Williams and Bloch, 1999a;Rybakova et al., 2000). Costameres and the connections between the contractile apparatus and the sarcolemma that they anchor are present at the plasma membrane overlying both the Z and M lines of superficial myofibrils of fast-twitch muscles (Porter et al., 1992;Williams et al., 2000). They also can be oriented at the plasma membrane parallel to the longitudinal axis of the myofibers, creating a rectilinear, structural lattice at the sarcolemma. Dystrophin and its associated proteins are enriched at all these sites (Porter et al., 1992;Williams and Bloch, 1999a;Williams et al...

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Section: Overexpression Of K8 and K19 In Muscle Fibersmentioning

confidence: 99%

Specific Interaction of the Actin-binding Domain of Dystrophin with Intermediate Filaments Containing Keratin 19

Stone

O’Neill

Catino

et al. 2005

MBoC

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“…Small ankyrin 1 (sAnk1, Ank1.5) (Bagnato et al, 2003;Birkenmeier et al, 1998), a small (,20 kDa) protein of striated muscle (Zhou et al, 1997), is a product of the ANK1 gene and shares homology with larger members of the ankyrin superfamily (Birkenmeier et al, 1998;Borzok et al, 2007). Ankyrins are ubiquitously expressed proteins that typically function to link integral membrane proteins to cytoskeletal components.…”

Section: Introductionmentioning

confidence: 99%

Integrity of the network sarcoplasmic reticulum in skeletal muscle requires small ankyrin 1

Ackermann

Ziman

Strong

et al. 2011

Journal of Cell Science

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SummarySmall ankyrin 1 (sAnk1; Ank1.5) is a ,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 Ca 2+ 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 Ca 2+ 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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“…Although the ANK1 and ANK2 gene products are largely restricted to red cells and brain, respectively, the ANK3 gene transcribes isoforms that display a general tissue distribution and are hence termed AnkG. These include a 480-kD isoform localized at the axonal initial segment and node of Ranvier (6), a 190/210-kD kidney ankyrin isoform expressed at the plasma membranes of kidney tubule cells (7,8), and truncated isoforms associated with the Golgi apparatus (9,10), lysosomes (11), and sarcoplasmic reticulum (12). The majority of ankyrins described to date are modular proteins comprising three conserved domains, including an aminoterminal domain containing a varying number of ankyrin repeats, a spectrin-binding domain, and a death domain located near the carboxyl terminal (1)(2)(3)(4)(5)(6)(7)(8).…”

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confidence: 99%

The Death Domain of Kidney Ankyrin Interacts with Fas and Promotes Fas-Mediated Cell Death in Renal Epithelia

Río¹,

Imam²,

DeLeon³

et al. 2004

Journal of the American Society of Nephrology

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Abstract. Ankyrins are a ubiquitously expressed family of conserved proteins that mediate the linkage of integral membrane proteins such as transporters and channels with the underlying cytoskeleton. Ankyrins possess a conserved death domain, the functional significance of which has remained puzzling. In this study, the death domain of AnkG190, the isoform of ankyrin expressed in kidney tubules, was used as bait in a yeast two-hybrid screen to identify interacting partners. One of these interactions was with the proapoptotic molecule Fas. This was confirmed by coimmunoprecipitation, colocalization, and glutathione S-transferase pull-down assays in cultured renal epithelial (MDCK) cells. Site-directed mutagenesis of a conserved arginine (R1496 in AnkG190), previously shown to be critical for the binding of Fas (R234 in Fas) to FADD, abolished the interaction of ankyrin's death domain with Fas. Overexpression of constructs containing ankyrin's death domain promoted Fas-mediated apoptosis in MDCK cells. The linkage between ankyrin and Fas was confirmed in vivo in mouse kidney tubule cells by coimmunoprecipitation and colocalization. In an established mouse model of renal ischemia-reperfusion injury characterized by apoptotic tubule cell death, the expression of both ankyrin and Fas was markedly induced, and the interaction between these molecules remained intact. The results identify a novel tethering interaction between ankyrin and Fas in kidney epithelia and suggest that AnkG190 may play a role as an adapter molecule in renal tubule cell death.Tethering interactions between membrane proteins and the underlying spectrin-based cytoskeleton play key roles in several cellular activities, including organization of plasma membrane domains (1

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Small, Membrane-bound, Alternatively Spliced Forms of Ankyrin 1 Associated with the Sarcoplasmic Reticulum of Mammalian Skeletal Muscle

Cited by 89 publications

References 61 publications

Specific Interaction of the Actin-binding Domain of Dystrophin with Intermediate Filaments Containing Keratin 19

Specific Interaction of the Actin-binding Domain of Dystrophin with Intermediate Filaments Containing Keratin 19

Integrity of the network sarcoplasmic reticulum in skeletal muscle requires small ankyrin 1

The Death Domain of Kidney Ankyrin Interacts with Fas and Promotes Fas-Mediated Cell Death in Renal Epithelia

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