Ank3 (epithelial ankyrin), a widely distributed new member of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain.

Peters, Luanne L.; John, Kathryn M.; Lu, Frederick M.; Eicher, Eva M.; Higgins, A; Yialamas, M; Turtzo, LC; Otsuka, Anthony J.; Lux, Samuel E.

doi:10.1083/jcb.130.2.313

Cited by 153 publications

(160 citation statements)

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“…Presently, at least three ankyrin genes have been identified: ankyrin 1 (Ank 1 or ankyrin R ), ankyrin 2 (Ank 2 or ankyrin B ), and ankyrin 3 (Ank 3 or ankyrin G ; Lux et al 1990; Otto et al 1991; Kordeli et al 1995; Peters et al 1995). These molecules belong to a family of related genes that probably arose by duplication and divergence of a common ancestral gene.…”

Section: Discussionmentioning

confidence: 99%

“…Rabbit anti-ANK3 antibody was provided by Dr. L.L. Peters (Jackson Laboratory, Bar Harbor, ME; Peters et al 1995). …”

Section: Methodsmentioning

confidence: 99%

“…Two pGEX-2TK recombinant plasmids pA3-79 (expressing epithelial Ank3 NH 2 -terminal 1–455 amino acids) and pA3-88 (expressing epithelial Ank3 NH 2 -terminal 317–834 amino acids; Peters et al 1995) were provided by Dr. L.L. Peters from the Jackson Laboratory.…”

Section: Methodsmentioning

confidence: 99%

“…Presently, at least three ankyrin genes have been identified: ankyrin 1 (ANK1 or ankyrin R ), ankyrin 2 (ANK2 or ankyrin B), and ankyrin 3 (ANK3 or ankyrin G ) (Lambert et al 1990; Lux et al 1990; Tse et al 1991; Otto et al 1991; Peters and Lux 1993; Kordeli et al 1995; Peters et al 1995). All ankyrin species (e.g., ANK1, ANK2, and ANK3) are monomers comprised of two highly conserved domains and a variable domain.…”

Section: Introductionmentioning

confidence: 99%

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Ankyrin–Tiam1 Interaction Promotes Rac1 Signaling and Metastatic Breast Tumor Cell Invasion and Migration

Bourguignon

Zhu

Shao

et al. 2000

The Journal of Cell Biology

116

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Tiam1 (T-lymphoma invasion and metastasis 1) is one of the known guanine nucleotide (GDP/GTP) exchange factors (GEFs) for Rho GTPases (e.g., Rac1) and is expressed in breast tumor cells (e.g., SP-1 cell line). Immunoprecipitation and immunoblot analyses indicate that Tiam1 and the cytoskeletal protein, ankyrin, are physically associated as a complex in vivo. In particular, the ankyrin repeat domain (ARD) of ankyrin is responsible for Tiam1 binding. Biochemical studies and deletion mutation analyses indicate that the 11–amino acid sequence between amino acids 717 and 727 of Tiam1 (717GEGTDAVKRS727L) is the ankyrin-binding domain. Most importantly, ankyrin binding to Tiam1 activates GDP/GTP exchange on Rho GTPases (e.g., Rac1).Using an Escherichia coli–derived calmodulin-binding peptide (CBP)–tagged recombinant Tiam1 (amino acids 393–728) fragment that contains the ankyrin-binding domain, we have detected a specific binding interaction between the Tiam1 (amino acids 393–738) fragment and ankyrin in vitro. This Tiam1 fragment also acts as a potent competitive inhibitor for Tiam1 binding to ankyrin. Transfection of SP-1 cell with Tiam1 cDNAs stimulates all of the following: (1) Tiam1–ankyrin association in the membrane projection; (2) Rac1 activation; and (3) breast tumor cell invasion and migration. Cotransfection of SP1 cells with green fluorescent protein (GFP)–tagged Tiam1 fragment cDNA and Tiam1 cDNA effectively blocks Tiam1–ankyrin colocalization in the cell membrane, and inhibits GDP/GTP exchange on Rac1 by ankyrin-associated Tiam1 and tumor-specific phenotypes. These findings suggest that ankyrin–Tiam1 interaction plays a pivotal role in regulating Rac1 signaling and cytoskeleton function required for oncogenic signaling and metastatic breast tumor cell progression.

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Section: Discussionmentioning

confidence: 99%

“…Rabbit anti-ANK3 antibody was provided by Dr. L.L. Peters (Jackson Laboratory, Bar Harbor, ME; Peters et al 1995). …”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Ankyrin–Tiam1 Interaction Promotes Rac1 Signaling and Metastatic Breast Tumor Cell Invasion and Migration

Bourguignon

Zhu

Shao

et al. 2000

The Journal of Cell Biology

116

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“…The possibility that lateral membranes of epithelial cells have a spectrin-based membrane skeleton similar to erythrocytes has been suggested by localization of isoforms of spectrin and ankyrin at sites of cell-cell contact (Drenckhahn et al, 1985;Nelson and Veshnock, 1986;Drenckhahn and Bennett, 1987;Peters et al, 1995). Moreover, resident lateral membrane proteins including the Na/K ATPase and E-cadherin either bind directly or coimmunoprecipitate with ankyrin and spectrin (Nelson and Veshnock, 1987;Nelson and Hammerton, 1989;Nelson et al, 1990;Morrow et al, 1989;Davis and Bennett, 1990).…”

Section: Introductionmentioning

confidence: 99%

Adducin Promotes Micrometer-Scale Organization of β2-Spectrin in Lateral Membranes of Bronchial Epithelial Cells

Abdi

Bennett

2008

MBoC

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Adducin promotes assembly of spectrin-actin complexes, and is a target for regulation by calmodulin, protein kinase C, and rho kinase. We demonstrate here that adducin is required to stabilize preformed lateral membranes of human bronchial epithelial (HBE) cells through interaction with ␤2-spectrin. We use a Tet-on regulated inducible small interfering RNA (siRNA) system to deplete ␣-adducin from confluent HBE cells. Depletion of ␣-adducin resulted in increased detergent solubility of spectrin after normal membrane biogenesis during mitosis. Conversely, depletion of ␤2-spectrin resulted in loss of adducin from the lateral membrane. siRNA-resistant ␣-adducin prevented loss of lateral membrane, but only if ␣-adducin retained the MARCKS domain that mediates spectrin-actin interactions. Phosphomimetic versions of adducin with S/D substitutions at protein kinase C phosphorylation sites in the MARCKS domain were not active in rescue. We find that adducin modulates long-range organization of the lateral membrane based on several criteria. First, the lateral membrane of adducin-depleted cells exhibited reduced height, increased curvature, and expansion into the basal surface. Moreover, E-cadherin-GFP, which normally is restricted in lateral mobility, rapidly diffuses over distances up to 10 m. We conclude that adducin acting through spectrin provides a novel mechanism to regulate global properties of the lateral membrane of bronchial epithelial cells.

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The spectrin-based skeleton at the postsynaptic membrane of the neuromuscular junction

Kordeli

2000

Microsc. Res. Tech.

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Membrane skeletons, in particular the spectrin‐based skeleton, are thought to participate in the organization of specialized membrane domains by restricting integral proteins to specific membrane sites. In the neuromuscular junction, discrete isoforms of spectrin and ankyrin, the peripheral protein that links spectrin to the membrane, colocalize with voltage‐dependent sodium channels and N‐CAM at the troughs of the postsynaptic membrane folds. Moreover, β‐spectrin, N‐CAM, and sodium channels become clustered at the endplate during a period of time coincident with postsynaptic fold formation and synapse maturation. These observations suggest a role of the spectrin skeleton in directing and maintaining postsynaptic accumulations of sodium channels and N‐CAM. In addition, the coexistence of spectrin and dystrophin at the troughs of the junctional folds raises the question of their respective functions in this membrane domain, where both cytoskeletal proteins have the potential to associate with sodium channels via ankyrin and syntrophin, respectively. Possible scenarios are discussed here with respect to accumulating evidence from studies of assembly of similar membrane domains in neurons. Microsc. Res. Tech. 49:101–107, 2000. © 2000 Wiley‐Liss, Inc.

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Ank3 (epithelial ankyrin), a widely distributed new member of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain.

Abstract: Abstract. We cloned a novel ankyfin, Ank3, from mouse kidney cDNA. The full-length transcript is predicted to encode a 214-kD protein containing an 89 kD, NH2 terminal "repeat" domain; a 65 kD, central "spectrin-binding" domain; and a 56 kD, COOH-terminal

Cited by 153 publications

References 58 publications

Ankyrin–Tiam1 Interaction Promotes Rac1 Signaling and Metastatic Breast Tumor Cell Invasion and Migration

Ankyrin–Tiam1 Interaction Promotes Rac1 Signaling and Metastatic Breast Tumor Cell Invasion and Migration

Adducin Promotes Micrometer-Scale Organization of β2-Spectrin in Lateral Membranes of Bronchial Epithelial Cells

The spectrin-based skeleton at the postsynaptic membrane of the neuromuscular junction

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