Mode of Interactions of Human Aldolase Isozymes with Cytoskeletons

Kusakabe, Takahiro; Motoki, Kiyohisa; Hori, Katsuji

doi:10.1006/abbi.1997.0204

Cited by 73 publications

(66 citation statements)

References 34 publications

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“…The interaction of aldolase with actin can be modulated by aldolase substrates and products (27,28). We therefore sought to determine the allosteric effect of these and related molecules on the binding of aldolase to GST-G4 (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…In addition to its enzymatic activity, this protein plays a structural role in the binding and polymerization of actin (28,29,34). Depolymerization of the actin cytoskeleton with cytochalasin D or latrunculin B has been shown to attenuate insulin-stimulated GLUT4 translocation, suggesting that an intact actin cytoskeleton is required for insulin-stimulated GLUT4 translocation (30,31).…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Aldolase Mediates the Association of F-actin with the Insulin-responsive Glucose Transporter GLUT4

Kao¹,

Noda²,

Johnson³

et al. 1999

Journal of Biological Chemistry

112

104

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To identify potential proteins interacting with the insulin-responsive glucose transporter (GLUT4), we generated fusion proteins of glutathione S-transferase (GST) and the final 30 amino acids from GLUT4 (GST-G4) or GLUT1 (GST-G1). Incubation of these carboxylterminal fusion proteins with adipocyte cell extracts revealed a specific interaction of GLUT4 with fructose 1,6-bisphosphate aldolase. In the presence of aldolase, GST-G4 but not GST-G1 was able to co-pellet with filamentous (F)-actin. This interaction was prevented by incubation with the aldolase substrates, fructose 1,6-bisphosphate or glyceraldehyde 3-phosphate. Immunofluorescence confocal microscopy demonstrated a significant co-localization of aldolase and GLUT4 in intact 3T3L1 adipocytes, which decreased following insulin stimulation. Introduction into permeabilized 3T3L1 adipocytes of fructose 1,6-bisphosphate or the metabolic inhibitor 2-deoxyglucose, two agents that disrupt the interaction between aldolase and actin, inhibited insulin-stimulated GLUT4 exocytosis without affecting GLUT4 endocytosis. Furthermore, microinjection of an aldolase-specific antibody also inhibited insulin-stimulated GLUT4 translocation. These data suggest that aldolase functions as a scaffolding protein for GLUT4 and that glucose metabolism may provide a negative feedback signal for the regulation of glucose transport by insulin.The insulin-responsive glucose transporter GLUT4 is expressed primarily in adipose tissue, skeletal, and cardiac muscle (1-4). Under basal conditions, GLUT4 slowly recycles between poorly defined intracellular compartments and the plasma membrane with the vast majority sequestered in these intracellular storage sites. Insulin stimulates a large increase in the rate of GLUT4 exocytosis concomitant with a smaller decrease in the rate of GLUT4 endocytosis (5-7). The overall insulin-induced changes in GLUT4 trafficking kinetics result in a 10 -20-fold increase in the number of cell surface GLUT4 proteins that accounts for the majority of insulin-stimulated increases in glucose transport activity (8,9).Recently, several laboratories have begun to examine the subcellular distribution of GLUT4 to identify the mechanism responsible for the intracellular sequestration of the GLUT4 protein. Steady-state and kinetic analysis of various expressed GLUT4 chimeric proteins have indicated that both the aminoand carboxyl-terminal domains are important in GLUT4 internalization from the plasma membrane (10 -15). In particular, the carboxyl-terminal dileucine motif (SLL) was found to substantially alter GLUT4 trafficking kinetics and steady-state localization (16,17). Although a specific GLUT4 sequence responsible for intracellular localization has yet to be identified, the presence of a carboxyl-terminal retention signal is consistent with the observation that expression of the GLUT4 carboxyl-terminal domain results in the translocation of the endogenous GLUT4 protein to the plasma membrane (18). In addition, the presence of a GLUT4 carboxyl-terminal binding protein...

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Aldolase Mediates the Association of F-actin with the Insulin-responsive Glucose Transporter GLUT4

Kao¹,

Noda²,

Johnson³

et al. 1999

Journal of Biological Chemistry

112

104

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“…Indeed, recent work identified aldolase as a protein that interacts with the T. gondii MIC2 cytoplasmic domain and P. falciparum TRAP cytoplasmic domain (D. Sibley, personal communication). It is well established that aldolase of mammalian cells interacts with the actin cytoskeleton (Kusakabe et al, 1997;Schindler et al, 2001). Hence, aldolase is probably the bridge linking the cytoplasmic domains of TRAP-like proteins to the parasites' actin filaments.…”

Section: Discussionmentioning

confidence: 99%

Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex ofPlasmodiumsporozoites

Bergman

Kaiser

Fujioka

et al. 2003

Journal of Cell Science

186

172

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Apicomplexan host cell invasion and gliding motility depend on the parasite's actomyosin system located beneath the plasma membrane of invasive stages. Myosin A (MyoA), a class XIV unconventional myosin, is the motor protein. A model has been proposed to explain how the actomyosin motor operates but little is known about the components, topology and connectivity of the motor complex. Using the MyoA neck and tail domain as bait in a yeast two-hybrid screen we identified MTIP, a novel 24 kDa protein that interacts with MyoA. Deletion analysis shows that the 15 amino-acid C-terminal tail domain of MyoA, rather than the neck domain, specifically interacts with MTIP. In Plasmodium sporozoites MTIP localizes to the inner membrane complex (IMC), where it is found clustered with MyoA. The data support a model for apicomplexan motility and invasion in which the MyoA motor protein is associated via its tail domain with MTIP, immobilizing it at the outer IMC membrane. The head domain of the immobilized MyoA moves actin filaments that,directly or via a bridging protein, connect to the cytoplasmic domain of a transmembrane protein of the TRAP family. The actin/TRAP complex is then redistributed by the stationary MyoA from the anterior to the posterior end of the zoite, leading to its forward movement on a substrate or to penetration of a host cell.

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“…Aldolase C may also have moonlighting activities in establishing subsets of neurons during cerebellar development (Hawkes et al, 1993;Ahn et al, 1994) or during differentiation of progenitor cells in the subventricular zones of the developing brain (Staugaitis et al, 2001). Like neurofilament transcripts, aldolases A and C are expressed early in embryonic development, are upregulated during postnatal life (Kusakabe et al, 1997;Shiokawa et al, 2002), and are also differentially expressed in complementary cell types (Walther et al, 1998). Aldolase binds to the actin cytoskeleton and mediates the association of F-actin with the insulin-responsive glucose transporter GLUT4 (Kusakabe et al, 1997;Wang et al, 1997;Kao et al, 1999;Jewet and Sibley, 2003); however, the association with a neuronal mRNA was only recently uncovered (Cañete-Soler et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

Aldolases A and C Are Ribonucleolytic Components of a Neuronal Complex That Regulates the Stability of the Light-Neurofilament mRNA

Cañete‐Soler¹,

Reddy²,

Tolan³

et al. 2005

J. Neurosci.

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Mode of Interactions of Human Aldolase Isozymes with Cytoskeletons

Cited by 73 publications

References 34 publications

Aldolase Mediates the Association of F-actin with the Insulin-responsive Glucose Transporter GLUT4

Aldolase Mediates the Association of F-actin with the Insulin-responsive Glucose Transporter GLUT4

Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex ofPlasmodiumsporozoites

Aldolases A and C Are Ribonucleolytic Components of a Neuronal Complex That Regulates the Stability of the Light-Neurofilament mRNA

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