An Alternative First Exon in the Distal End of the Erythroid Ankyrin Gene Leads to Production of a Small Isoform Containing an NH2-Terminal Membrane Anchor

Birkenmeier, Connie S.; Sharp, John J.; Gifford, Elaine J; Deveau, Susan A.; Barker, Jane E.

doi:10.1006/geno.1998.5305

Cited by 42 publications

(48 citation statements)

References 47 publications

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“…The data presented here indicate that the ankyrin 5′HS region is a barrier insulator in erythroid cells. In addition to the erythroid promoter, there are at least three other ankyrin-1 promoters, one approximately 40 kb 5′ of the erythroid promoter directing transcripts in neural and muscle cells, one approximately 16 kb 3′ of the erythroid promoter directing transcripts in cerebellar cells, and one approximately 200 kb 3′ of the erythroid promoter directing transcripts in skeletal muscle (62)(63)(64)(65)(66). Thus, it is not surprising that tissue-specific barrier insulators are required in the ankyrin-1 locus to prevent ectopic expression or silencing of tissue-specific transcripts.…”

Section: Discussionmentioning

confidence: 99%

Mutation of a barrier insulator in the human ankyrin-1 gene is associated with hereditary spherocytosis

Gallagher¹,

Steiner²,

Liem³

et al. 2010

J. Clin. Invest.

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Section: Discussionmentioning

confidence: 99%

Mutation of a barrier insulator in the human ankyrin-1 gene is associated with hereditary spherocytosis

Gallagher¹,

Steiner²,

Liem³

et al. 2010

J. Clin. Invest.

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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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“…This specialization appears to have evolved from the tissue-specific, developmentally regulated expression of multiple protein isoforms. Ankyrin isoform diversity arises from different gene products, from differential, alternative splicing of the same gene product, from alternate polyadenylation, from the use of tissue-specific promoters, and/or the use of alternate NH 2 or COOH-termini [14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29]. Although numerous ankyrin-1 isoforms are visualized on Western blots of erythrocyte membranes [16], it is unknown if isoforms of ankyrin-1 are generated in erythroid cells by use of alternate translation initiation codons.…”

Section: Introductionmentioning

confidence: 99%

Ankyrin‐linked hereditary spherocytosis in an African–American kindred

et al. 2008

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Mutations of ankyrin-1 are the most frequent cause of the inherited hemolytic anemia, hereditary spherocytosis (HS), in people of European ancestry. Ankyrin-1, which provides the primary linkage between the erythrocyte membrane skeleton and the plasma membrane, has numerous isoforms generated by alternative splicing, alternate polyadenylation, use of tissue-specific promoters, and alternate NH 2 or COOH-termini. Mutation detection in erythrocyte membrane protein genes, including ankyrin, has been a challenge, primarily due to the large size of these genes, and the apparent frequent occurrence of HS-associated null alleles. Using denaturing high-performance liquid chromatography (DHPLC), we screened the ankyrin gene of the proband of a large, three generation African-American kindred with ankyrin-deficient HS. DHPLC yielded an abnormal chromatogram for exon 1. Examination of the corresponding exon 1 sequence in genomic DNA from the proband revealed heterozygosity for a mutation of the initiator methionine (ATG to ATA Met 1 Ile). Coupled in vitro transcription/translation studies with rabbit reticulocyte lysates demonstrated that the wild-type ankyrin erythroid cDNA initiates only from the known initiator methionine, indicating that the use of alternate initiator methionine is not a mechanism of isoform diversity in erythroid cells. The mutant ankyrin allele, unlike some initiator methionine mutations that utilize downstream codons for translation initiation, was associated with a null allele. This is the first report describing ankyrin-linked HS in an African-American kindred. Am. J. Hematol. 83:789-794, 2008. V

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An Alternative First Exon in the Distal End of the Erythroid Ankyrin Gene Leads to Production of a Small Isoform Containing an NH2-Terminal Membrane Anchor

Cited by 42 publications

References 47 publications

Mutation of a barrier insulator in the human ankyrin-1 gene is associated with hereditary spherocytosis

Mutation of a barrier insulator in the human ankyrin-1 gene is associated with hereditary spherocytosis

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

Ankyrin‐linked hereditary spherocytosis in an African–American kindred

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