Molecular Cloning and Characterization of a Tumor Rejection Antigen from Rat Histiocytoma, AK-5

Muralikrishna, T.; Begum, Zareena; Swamy, Ch.V.B.; Khar, Ashok

doi:10.1089/dna.1998.17.603

Cited by 5 publications

(6 citation statements)

References 23 publications

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“…(39) A partial sequence of coronin 7 has been previously identified as a histiocytoma-specific p70 antigen strongly expressed in the rat thymus, spleen and brain. (40) This expression pattern is consistent with our data on full-length coronin 7 (crn7). (39) We showed that, in contrast to cytosolic coronin 3, cytosolic crn7 is not phosphorylated, while the membrane-associated pool is phosphorylated on tyrosine residues suggesting that crn7 is recruited from the cytosol to Golgi membranes upon tyrosine phosphorylation.…”

Section: Mammalian Coronin 7 Has No Cytoskeleton-related Functions Busupporting

confidence: 92%

Coronin proteins as multifunctional regulators of the cytoskeleton and membrane trafficking

2005

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Coronins constitute an evolutionarily conserved family of WD-repeat actin-binding proteins, which can be clearly classified into two distinct groups based on their structural features. All coronins possess a conserved basic N-terminal motif and three to ten WD repeats clustered in one or two core domains. Dictyostelium and mammalian coronins are important regulators of the actin cytoskeleton, while the fly Dpod1 and the yeast coronin proteins crosslink both actin and microtubules. Apart from that, several coronins have been shown to be involved in vesicular transport. C. elegans POD-1 and Drosophila coro regulate the actin cytoskeleton, but also govern vesicular trafficking as indicated by mutant phenotypes. In both organisms, defects in cytoskeleton and trafficking lead to severe developmental defects ranging from abnormal cell division to aberrant formation of morphogen gradients. Finally, mammalian coronin 7 appears not to execute any cytoskeleton-related functions, but rather participates in regulating Golgi trafficking. Here, we review recent data providing more insight into molecular mechanisms underlying the regulation of F-actin structures, cytoskeletal rearrangements and intracellular membrane transport by coronin proteins and the way that they might link cytoskeleton with trafficking in development and disease.

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Section: Mammalian Coronin 7 Has No Cytoskeleton-related Functions Busupporting

confidence: 92%

Coronin proteins as multifunctional regulators of the cytoskeleton and membrane trafficking

2005

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“…The AK-5 tumor shows a particular growth pattern when transplanted subcutaneously. The tumor grows rapidly during the growth phase (days 1-14), after which necrotic spots appear and the tumor undergoes rejection (days 15-25) followed by the healing phase (days [25][26][27][28][29][30][31][32][33][34][35] when the wound heals and the animals become totally normal and are immunized against AK-5 tumor (7).…”

Section: Cellular Influx Into the Peritoneal Compartmentmentioning

confidence: 99%

Migration of antigen presenting cells from periphery to the peritoneum during an inflammatory response: role of chemokines and cytokines

et al. 2004

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We demonstrate the migration of antigen presenting cells (APCs), macrophages, and dendritic cells from the subcutaneous site to the peritoneum after they have picked up the antigen, using cell tracking dye. The migration of the APCs is more universal as it was also observed after injection of MethA tumor, DH-5alpha cells, and leishmania parasites, in addition to AK-5 tumor cells. Cellular migration is mediated by several chemokines and cytokines that also induce heavy influx of immune cells into the peritoneum. MIP-3beta secreted by the mesothelial cells is involved in the cellular influx into the peritoneum, whereas IL-12 and IFN-gamma produced by the APCs induced activation of immune cells in the peritoneum. Our results suggest an antigen presentation function for the APCs in the peritoneum as studied by lymphoproliferation assays. These studies indicate antigen presentation function of the activated migratory APCs from the distant subcutaneous site to the peritoneum, suggesting it acts as an important lymphoid organ involved in the enhancement of effector cell function.

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“…The coiled-coil domain of p57/coronin-1 includes a so-called leucine zipper motif, with four leucine residues that appear every seven amino acid residues [6]. Because the leucine zipper motif is not found in other mammalian coronin members [16,[20][21][22][23][24], we reasoned that it may serve a function unique to p57/coronin-1, and tested the hypothesis that the leucine zipper motif mediates homodimer formation.…”

Section: Introductionmentioning

confidence: 99%

Homotypic dimerization of the actin-binding protein p57/coronin-1 mediated by a leucine zipper motif in the C-terminal region

Oku

Itoh

Ishii

et al. 2005

Biochemical Journal

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The actin-binding protein p57/coronin-1, a member of the coronin protein family, is selectively expressed in immune cells, and has been implicated in leucocyte migration and phagocytosis by virtue of its interaction with F-actin (filamentous actin). We previously identified two sites in the N-terminal region of p57/coronin-1 by which it binds actin, and in the present study we examine the role of the leucine zipper motif located in the C-terminal coiled-coil domain in mediating the homotypic association of p57/coronin-1. Recombinant p57/coronin-1 protein in solution formed a homodimer, as analysed by Superose 12 column chromatography and by sucrose density gradient centrifugation. In vivo, a truncated form consisting of the C-terminal coiled-coil domain co-precipitated with full-length p57/coronin-1 when both were co-expressed in COS-1 cells. A chimaeric construct composed of the C-terminal domain of p57/coronin-1 (which lacks the actin-binding sites) fused with green fluorescent protein co-localized with cortical F-actin-rich regions in COS-1 cells only when full-length p57/coronin-1 was expressed simultaneously in the cells, suggesting that the C-terminal region is required for the homotypic association of p57/coronin-1. Furthermore, p57LZ, a polypeptide consisting of the C-terminal 90 amino acid residues of p57/coronin-1, was sufficient for dimerization. When two leucine residues out of the four that constitute the leucine zipper structure in p57LZ or full-length p57 were replaced with alanine residues, the mutants failed to form homodimers. Taken together, these results demonstrate that p57/coronin-1 forms homodimers, that the association is mediated by the leucine zipper structure in the C-terminal region, and that it plays a role in the cross-linking of F-actin in the cell.

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Molecular Cloning and Characterization of a Tumor Rejection Antigen from Rat Histiocytoma, AK-5

Cited by 5 publications

References 23 publications

Coronin proteins as multifunctional regulators of the cytoskeleton and membrane trafficking

Coronin proteins as multifunctional regulators of the cytoskeleton and membrane trafficking

Migration of antigen presenting cells from periphery to the peritoneum during an inflammatory response: role of chemokines and cytokines

Homotypic dimerization of the actin-binding protein p57/coronin-1 mediated by a leucine zipper motif in the C-terminal region

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