Filamin-A Binds to the Carboxyl-terminal Tail of the Calcium-sensing Receptor, an Interaction That Participates in CaR-mediated Activation of Mitogen-activated Protein Kinase

Hjälm, Göran; Macleod, John; Kifor, Olga; Chattopadhyay, Naibedya; Brown, Edward M.

doi:10.1074/jbc.m100784200

Cited by 169 publications

(142 citation statements)

References 27 publications

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“…These authors suggested that CaR may engage the MAP kinase or other signaling pathways through this scaffolding protein and lead to subsequent activation of Rho GTPases. Hjälm et al (39) proposed that a 91-aa segment (907-997) of the hCaR C-terminal ICD includes the filamin-binding domain. This segment of the hCaR corresponds to the C-terminal-most regions of the teleost CaRs, beginning presumably at residue 891 in tCaR.…”

Section: Resultsmentioning

confidence: 99%

cDNA Cloning and Functional Expression of a Ca2+-sensing Receptor with Truncated C-terminal Tail from the Mozambique Tilapia (Oreochromis mossambicus)

Loretz¹,

Pollina

Hyodo

et al. 2004

Journal of Biological Chemistry

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The complete cDNA sequence of the tilapia extracellular Ca 2؉ -sensing receptor (CaR) was determined. The transcript length of tilapia CaR (tCaR) is 3.4 kbp and encodes a 940-amino acid, 7-transmembrane domain protein that is consistent in its structural features with known mammalian and piscine CaRs. The tCaR extracellular domain includes a characteristic hydrophobic segment, conserved cysteine residues that are implicated in receptor dimerization (Cys 129 and Cys 131 ) and in coupling to the transmembrane domain (nine conserved cysteine residues), and conserved serine residues (Ser 147 and The roles for ionic calcium (Ca 2ϩ ) in physiological functions are many and varied and essential for survival. Ca 2ϩ -dependent cellular processes include hormone secretion (stimulussecretion coupling), excitability and cell motility (excitationcontraction coupling), and neurotransmission (Ca 2ϩ -based action potentials). This critical involvement of Ca 2ϩ in these and other cellular functions is unique among ions. Ca 2ϩ is simultaneously a controlled variable in physiological systems, an extracellular messenger in multicellular organisms, and an intracellular mediator in a variety of effector cells.Unicellular organisms acquire Ca 2ϩ from the external environment; they have little control over the composition of the surrounding medium and thus had to evolve plasma membrane-bound and other cellular mechanisms to realize cellular Ca 2ϩ homeostasis eventually permitting some degree of habitat survival and selection. In multicellular organisms, active regulation by integumentary tissues of the composition of an "extracellular fluid," which bathes all cells, assures a constant internal milieu and contributes to normal Ca 2ϩ -dependent cell functions. In terrestrial vertebrates, Ca 2ϩ homeostasis depends upon appropriate dietary intake, renal output, and osseous storage and mobilization of Ca 2ϩ . These processes are well known and are regulated by parathyroid hormone, calcitonin, and 1,25-dihydroxyvitamin D acting on kidney, intestine, and bone. Activation of the Ca 2ϩ -sensing receptor (CaR) 1 by its natural ligand, extracellular Ca 2ϩ , alters parathyroid hormone and calcitonin secretion and inhibits renal 1-hydroxylase to retard the synthesis of 1,25-dihydroxyvitamin D (1, 2). Ca 2ϩ balance is achieved through regulated calciotropic hormone secretion in response to the extracellular Ca 2ϩ concentration ([Ca 2ϩ ] o ); the secreted hormones, in turn, control the activity of Ca 2ϩ -transporting tissues to bring about alterations in [Ca 2ϩ ] o . Interestingly, in fishes, the calcium homeostatic process involves ion-transporting tissues not represented in other vertebrate classes (viz., the mitochondria-rich "chloride cells" of the gills and skin) and a different panel of hormones (prolactin and somatolactin from the pituitary, and stanniocalcin from the piscine corpuscles of Stannius (3)). Opportunities for cutaneous

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Section: Resultsmentioning

confidence: 99%

cDNA Cloning and Functional Expression of a Ca2+-sensing Receptor with Truncated C-terminal Tail from the Mozambique Tilapia (Oreochromis mossambicus)

Loretz¹,

Pollina

Hyodo

et al. 2004

Journal of Biological Chemistry

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“…In addition, some studies have shown successful transduction of PTD-fusion proteins into cells without fixation [47,98,[158][159][160][161]. Further, many of these studies have also shown biological effects upon treatment with PTD-fusion proteins, which could be due to the interactions with surface receptors [162] or due to the release of proteins from lysosomes into the cytoplasm and nucleus. It has been demonstrated that PTD entry occurs via endosomal pathways through either caveolae [163,164] or macropinocytosis where lysosomotropic agents are required [126,157].…”

Section: Validation Of True Ptd-mediated Protein Transductionmentioning

confidence: 99%

The taming of the cell penetrating domain of the HIV Tat: Myths and realities

Chauhan

Tikoo²,

Kapur

et al. 2007

Journal of Controlled Release

156

136

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Protein transduction with cell penetrating peptides over the past several years has been shown to be an effective way of delivering proteins in vitro and now several reports have also shown valuable in vivo applications in correcting disease states. An impressive bioinspired phenomenon of crossing biological barriers came from HIV transactivator Tat protein. Specifically, the protein transduction domain of HIV-Tat has been shown to be a potent pleiotropic peptide in protein delivery. Various approaches such as molecular modeling, arginine guanidinium head group structural strategy, multimerization of PTD sequence and phage display system have been applied for taming of the PTD. This has resulted in identification of PTD variants which are efficient in cell membrane penetration and cytoplasmic delivery. Inspite of these state of the art technologies, the dilemma of low protein transduction efficiency and target specific delivery of PTD fusion proteins remains unsolved. Moreover, some misconceptions about PTD of Tat in the literature require considerations. We have assembled critical information on secretory, plasma membrane penetration and transcellular properties of Tat and PTD using molecular analysis and available experimental evidences.

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“…Filamin A is known to bind to various membrane and signaling molecules, see reviews (Stossel et al, 2001;van der Flier and Sonnenberg, 2001)}. More recently different laboratories, including our own, demonstrated that filamin A associates with various GPCRs, such as the D2 and D3 dopamine receptors (Li et al, 2000;Lin et al, 2001), the calcium-sensing receptor (CaR) (Awata et al, 2001;Hjalm et al, 2001), the metabotropic glutamate receptor type 7 (Enz, 2002), alpha1-adrenergic receptors (Zhang et al, 2004), calcitonin receptor (Seck et al, 2003) and the mu opioid receptor (MOP) (Onoprishvili et al, 2003). In some cases, such as the calcium sensing receptor and the MOP, the binding of filamin A is to the carboxyl tail, while for other receptors, such as the D2 and D3 dopamine receptors, the binding is to the third cytoplasmic loop.…”

Section: Introductionmentioning

confidence: 99%

Chronic morphine treatment up-regulates mu opioid receptor binding in cells lacking filamin A

Onoprishvili

Simon

2007

Brain Research

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We investigated the effects of morphine and other agonists on the human mu opioid receptor (MOP) expressed in M2 melanoma cells, lacking the actin cytoskeleton protein filamin A and in A7, a sub clone of the M2 melanoma cells, stably transfected with filamin A cDNA. The results of binding experiments showed, that after chronic morphine treatment (24 hr) of A7 cells, MOP binding sites were down-regulated to 63% of control, whereas, unexpectedly, in M2 cells, MOP binding was upregulated to 188% of control naïve cells. Similar up-regulation was observed with the agonists methadone and levorphanol. The presence of antagonists (naloxone or CTAP) during chronic morphine treatment inhibited MOP down-regulation in A7 cells. In contrast, morphine-induced upregulation of MOP in M2 cells was further increased by these antagonists. Chronic morphine desensitized MOP in A7 cells, i.e. it decreased DAMGO-induced stimulation of GTPγS binding. In M2 cells DAMGO stimulation of GTPγS binding was significantly greater than in A7 cells and was not desensitized by chronic morphine. Pertussis toxin treatment abolished morphine-induced receptor up-regulation in M2 cells, whereas it had no effect on morphine-induced down-regulation in A7 cells. These results indicate that, in the absence of filamin A, chronic treatment with morphine, methadone or levorphanol leads to up-regulation of MOP, to our knowledge, the first instance of opioid receptor up-regulation by agonists in cell culture.

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Filamin-A Binds to the Carboxyl-terminal Tail of the Calcium-sensing Receptor, an Interaction That Participates in CaR-mediated Activation of Mitogen-activated Protein Kinase

Cited by 169 publications

References 27 publications

cDNA Cloning and Functional Expression of a Ca2+-sensing Receptor with Truncated C-terminal Tail from the Mozambique Tilapia (Oreochromis mossambicus)

cDNA Cloning and Functional Expression of a Ca2+-sensing Receptor with Truncated C-terminal Tail from the Mozambique Tilapia (Oreochromis mossambicus)

The taming of the cell penetrating domain of the HIV Tat: Myths and realities

Chronic morphine treatment up-regulates mu opioid receptor binding in cells lacking filamin A

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