ArticleThe Journal of cell biology1997
Isoforms of ankyrin-3 that lack the NH2-terminal repeats associate with mouse macrophage lysosomes.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 72 citations in OpenAlex.
- A modified density gradient proteomic-based method to analyze endolysosomal proteins in cardiac tissue.iScience · 2021Article
- Roles of palmitoylation in structural long-term synaptic plasticity.Molecular brain · 2021Review
- Human ankyrins and their contribution to disease biology: An update.Journal of biosciences · 2020Review
- Ankyrins: Roles in synaptic biology and pathology.Molecular and cellular neurosciences · 2018Review
- Ankyrin G expression is associated with androgen receptor stability, invasiveness, and lethal outcome in prostate cancer patients.Journal of molecular medicine (Berlin, Germany) · 2016Article
- Isoforms of Spectrin and Ankyrin Reflect the Functional Topography of the Mouse Kidney.PloS one · 2016Article
- Bioinformatics approach to predict target genes for dysregulated microRNAs in hepatocellular carcinoma: study on a chemically-induced HCC mouse model.BMC bioinformatics · 2015Article
- Ankyrin-G palmitoylation and βII-spectrin binding to phosphoinositide lipids drive lateral membrane assembly.The Journal of cell biology · 2014Article
- Genome-wide study identifies two loci associated with lung function decline in mild to moderate COPD.Human genetics · 2013Article
- Ankyrin 3: genetic association with bipolar disorder and relevance to disease pathophysiology.Biology of mood & anxiety disorders · 2012Article
- Immune and inflammatory pathways are involved in inherent bone marrow ossification.Clinical orthopaedics and related research · 2012Article
- Membrane domains based on ankyrin and spectrin associated with cell-cell interactions.Cold Spring Harbor perspectives in biology · 2009Review
- Exon organization and novel alternative splicing of the human ANK2 gene: implications for cardiac function and human cardiac disease.Journal of molecular and cellular cardiology · 2008Article
- Obscurin is a ligand for small ankyrin 1 in skeletal muscle.Molecular biology of the cell · 2003Article
- Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated muscles.The Journal of cell biology · 2003Article
- Association of spectrin-like proteins with the actin-organized aggregate of endoplasmic reticulum in the Spitzenkörper of gravitropically tip-growing plant cells.Plant physiology · 2001Article
- betaIV spectrin, a new spectrin localized at axon initial segments and nodes of ranvier in the central and peripheral nervous system.The Journal of cell biology · 2000Article
- Human spectrin Src homology 3 domain binding protein 1 regulates macropinocytosis in NIH 3T3 cells.Journal of cell science · 2000Article
- ankA: an Ehrlichia phagocytophila group gene encoding a cytoplasmic protein antigen with ankyrin repeats.Infection and immunity · 2000Article
- Ankyrin-B is required for intracellular sorting of structurally diverse Ca2+ homeostasis proteins.The Journal of cell biology · 1999Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We have recently cloned and characterized ankyrin-3 (also called ankyrin(G)), a new ankyrin that is widely distributed, especially in epithelial tissues, muscle, and neuronal axons (Peters, L.L., K.M. John, F.M. Lu, E.M. Eicher, A. Higgins, M. Yialamas, L.C. Turtzo, A.J. Otsuka, and S.E. Lux. 1995. J. Cell Biol. 130: 313-330). Here we show that in mouse macrophages, ankyrin-3 is expressed exclusively as two small isoforms (120 and 100 kD) that lack the NH2-terminal repeats. Sequence analysis of isolated Ank3 cDNA clones, obtained by reverse transcription and amplification of mouse macrophage RNA (GenBank Nos. U89274 and U89275), reveals spectrin-binding and regulatory domains identical to those in kidney ankyrin-3 (GenBank No. L40631) preceded by a 29-amino acid segment of the membrane ("repeat") domain, beginning near the end of the last repeat. Antibodies specific for the regulatory and spectrin-binding domains of ankyrin-3 localize the protein to the surface of intracellular vesicles throughout the macrophage cytoplasm. It is not found on the plasma membrane. Also, epitope-tagged mouse macrophage ankyrin-3, transiently expressed in COS cells, associates with intracellular, not plasma, membranes. In contrast, ankyrin-1 (erythrocyte ankyrin, ankyrin(R)), which is also expressed in mouse macrophages, is located exclusively on the plasma membrane. The ankyrin-3-positive vesicles appear dark on phase-contrast microscopy. Two observations suggest that they are lysosomes. First, they are a late compartment in the endocytic pathway. They are only accessible to a fluorescent endocytic tracer (FITC-dextran) after a 24-h incubation, at which time all of the FITC-dextran-containing vesicles contain ankyrin-3 and vice versa. Second, the ankyrin-3-positive vesicles contain lysosomal-associated membrane glycoprotein (LAMP-1), a recognized lysosomal marker. This is the first evidence for the association of an ankyrin with lysosomes and is an example of two ankyrins present in the same cell that segregate to different locations.
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