Adducin in platelets: activation-induced phosphorylation by PKC and proteolysis by calpain

Gilligan, Diana M.; Sarid, Rami; Weese, Joleen

doi:10.1182/blood.v99.7.2418

Cited by 50 publications

(54 citation statements)

References 41 publications

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“…Phosphorylation by PKA, PKC, or calmodulin binding causes adducin to dissociate from actin filaments, whereas phosphorylation by Rho kinase increases affinity of adducin for actin filaments. In activated platelets, adducin is phosphorylated by PKC and becomes a better substrate for calpain proteolysis, suggesting that adducin complexes play a role in maintaining the shape of resting platelets but need to be removed from actin filaments during activation (Gilligan et al, 2002). Therefore, adducin could act as an intermediary between synaptic signaling and the resulting cytoskeletal plasticity.…”

Section: Discussionmentioning

confidence: 99%

Impaired Synaptic Plasticity and Learning in Mice Lacking β-Adducin, an Actin-Regulating Protein

Rabenstein¹,

Addy²,

Caldarone³

et al. 2005

J. Neurosci.

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The adducin family of proteins interacts with the actin cytoskeleton and the plasma membrane in a calcium-and cAMP-dependent manner. Thus, adducins may be involved in changes in cytoskeletal organization resulting from synaptic stimulation. ␤-Adducin knockout mice were examined in physiological and behavioral paradigms related to synaptic plasticity to elucidate the role the adducin family plays in processes underlying learning and memory. In situ hybridization for ␣-and ␤-adducin demonstrates that these mRNAs are found throughout the brain, with high levels of expression in the hippocampus. Schaffer collateral-CA1 tetanic long-term potentiation decayed rapidly in acute hippocampal slices from ␤-adducin knock-out mice, although baseline spine morphology and postsynaptic density were normal. Interestingly, the input-output relationship was significantly increased in hippocampal slices from ␤-adducin knock-out mice. Furthermore, ␤-adducin knock-out mice were impaired in performance of fear conditioning and the water maze paradigm. The current results indicate that ␤-adducin may play an important role in the cellular mechanisms underlying activitydependent synaptic plasticity associated with learning and memory.

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Section: Discussionmentioning

confidence: 99%

Impaired Synaptic Plasticity and Learning in Mice Lacking β-Adducin, an Actin-Regulating Protein

Rabenstein¹,

Addy²,

Caldarone³

et al. 2005

J. Neurosci.

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“…The adducins are actin-capping proteins that are involved in a variety of cellular signalling pathways ranging from cytoskeletal arrangements to apoptosis (Gilligan et al, 1999(Gilligan et al, , 2002Imamdi et al, 2004;Larsson, 2006;Matsuoka et al, 1996). Central to many aspects of adducin biology is its association with the dynactin complex.…”

Section: Discussionmentioning

confidence: 99%

“…Antisera to recombinant human erythrocyte a-adducin were used to examine the abundance of total a-adducin (Gilligan et al, 2002;Joshi et al, 1991). Monoclonal antibody directed at chlamydial Hsp60 was used to label and visualize chlamydial developmental forms (Yuan et al, 1992).…”

Section: Ser473mentioning

confidence: 99%

“…Infected and mock-infected cells were incubated at 37 uC in 5 % CO 2 . Protein samples used were prepared either by extraction of total cell proteins or by fractionation with Triton X-100 (Gilligan et al, 2002). For the Triton fractionation, infected and mock-infected cells were homogenized in lysis buffer, sonicated, centrifuged (16 000 g) and the Triton-soluble (TS) supernatant and Triton-insoluble pellet fractions were collected.…”

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Host α-adducin is redistributed and localized to the inclusion membrane in Chlamydia- and Chlamydophila-infected cells

et al. 2008

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A large-scale analysis of proteins involved in host-cell signalling pathways was performed using chlamydia-infected murine cells in order to identify host proteins that are differentially activated or localized following infection. Two proteins whose distribution was altered in Chlamydia trachomatis-infected cells relative to mock-infected cells were the actin-binding protein adducin and the regulatory kinase Raf-1. Immunoblot analysis with antibodies to both phosphorylated and non-phosphorylated forms of these proteins demonstrated that the abundance of each protein was markedly reduced in the cytosolic fraction of C. trachomatis-and Chlamydophila caviaeinfected cells, but the total cellular protein abundance remained unaffected by infection. Fluorescence microscopy of chlamydia-infected cells using anti-a-adducin antibodies demonstrated labelling at or near the chlamydial inclusion membrane. Treatment of infected cells with nocodazole or cytochalasin D did not affect a-adducin that was localized to the margins of the inclusion. The demonstration of a-adducin and Raf-1 redistribution within cells infected by different chlamydiae provides novel opportunities for analysis of host-pathogen interactions in this system.

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“…Various stimuli may lead to changes in the cellular distribution of spectrin, including its aggregation. Formation of aggregates was observed upon phosphorylation of adducin by PKC activated by phorbol-myristate acetate (PMA) [16,17] which resulted in the dissociation of spectrin from the spectrin-actin complex [18]. Aggregation of spectrin was also shown during induced hyperthermia [19] or lymphocyte activation [20], occurring concomitantly with PKC-b and PKC-θ activity.…”

Section: Introductionmentioning

confidence: 99%

PKC-θ is a negative regulator of TRAIL-induced and FADD-mediated apoptotic spectrin aggregation

Michalczyk

Toporkiewicz

Dubielecka

et al. 2015

Folia Histochem Cytobiol.

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Introduction. During studies on chemotherapy-induced apoptosis in lymphoid cells, we noted that aggregation of spectrin occurred early in apoptosis, i.e. before activation of initiator caspase(s) and prior to exposure of phosphatidylserine (PS). We also found that protein kinase C theta (PKC-θ) co-localized with spectrin in these aggregates. Our previously published studies indicated that in formation of early apoptotic spectrin aggregates, either PKC-θ or other apoptosis-related proteins are involved. Taking into consideration above data, we decided to test the effect of PKC-θ and Fas-associated death domain protein (FADD) on spectrin aggregation in these cells during tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis. Material and methods. For PKC-θ gene (PRKCQ) or FADD gene expression silencing in Jurkat T cells we used lentiviral particles containing shRNA and scrambled shRNA, respectively. Spectrin aggregates were detected by Western blotting after Triton-X 100 extraction in pellet and soluble fractions or by confocal imaging. Results. TRAIL-induced apoptosis results in spectrin aggregation and leads to translocation and aggregation of PKC-θ. We found that phorbol-myristate acetate, a PKC activator and translocation inducer, has only a small effect on spectrin aggregation. To further confirm this, we have also shown that knock down of PRKCQ in Jurkat T cells accelerates the formation of TRAIL-induced spectrin aggregates. Transient overexpression of the b-spectrin C-terminal fragment, containing multiple S/T phosphorylation sites, potential substrate sites for PKC-θ, accelerated the formation of spectrin aggregates. Silencing of downstream TRAIL receptor effector gene, FADD, delayed aggregation of spectrin, but did not reduce PKC-θ localization to the plasma membrane. Conclusions. In summary, our results show for the first time involvement of spectrin aggregation in TRAIL receptor-FADD apoptotic pathway and indicate that TRAIL-induced spectrin aggregate formation is mediated by FADD and negatively regulated by PKC-θ.

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Adducin in platelets: activation-induced phosphorylation by PKC and proteolysis by calpain

Cited by 50 publications

References 41 publications

Impaired Synaptic Plasticity and Learning in Mice Lacking β-Adducin, an Actin-Regulating Protein

Impaired Synaptic Plasticity and Learning in Mice Lacking β-Adducin, an Actin-Regulating Protein

Host α-adducin is redistributed and localized to the inclusion membrane in Chlamydia- and Chlamydophila-infected cells

PKC-θ is a negative regulator of TRAIL-induced and FADD-mediated apoptotic spectrin aggregation

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