VXFD in the Cytoplasmic Domain of Macrophage Scavenger Receptors Mediates Their Efficient Internalization and Cell-Surface Expression.

Morimoto, Kazunobu; Wada, Youichiro; Hinagata, Jun-ichi; Imanishi, Takeshi; Kodama, Tatsuhiko; Doi, Takefumi

doi:10.1248/bpb.22.1022

Cited by 21 publications

(20 citation statements)

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“…The KLKSFK motif may also be sufficient for cell surface trafficking of human SR-A, and the first 24 amino acids must be necessary for receptor internalization. The substitution of alanine for Val 21 , Phe 23 , or Asp 24 in hSR-A has been demonstrated to reduce both cell surface localization and internalization (20). However, those residues, named as a VXFD motif, may not be required for surface trafficking, because SR-A ⌬1-24 was sufficiently expressed on the cell surface in our study.…”

Section: Discussionmentioning

confidence: 65%

The Microtubule-binding Protein Hook3 Interacts with a Cytoplasmic Domain of Scavenger Receptor A

Sano

Ishino

Krämer

et al. 2007

Journal of Biological Chemistry

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The class A scavenger receptor (SR-A, and Asp 15 in the human SR-A cytoplasmic domain. By transfecting small interfering RNA targeting Hook3, total and surface expression, receptor-mediated ligand uptake and protein stability of SR-A were significantly promoted, whereas the protein synthesis and maturation were not altered. We propose for the first time that Hook3 may participate in the turnover of the endocytosed scavenger receptor.

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Section: Discussionmentioning

confidence: 65%

The Microtubule-binding Protein Hook3 Interacts with a Cytoplasmic Domain of Scavenger Receptor A

Sano

Ishino

Krämer

et al. 2007

Journal of Biological Chemistry

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“…A well defined internalization motif is not present in the cytoplasmic tail of SR-A. However, Morimoto et al (17) have suggested that a single motif, VXFD, is required for both SR-A internalization and cell-surface localization. In contrast, our results show that the membrane-proximal amino acids are sufficient for cellsurface localization, but that receptor internalization depends on a distinct motif, possibly the VXFD motif.…”

Section: Discussionmentioning

confidence: 99%

“…Previous studies have associated SR-A cell-surface localization and receptor internalization with a common cytoplasmic motif (17). However, the finding that SR-A ⌬1-49 localized to the cell surface, but did not internalize ligand, suggests that SR-A trafficking to the cell surface and internalization have distinct cytoplasmic requirements.…”

Section: The Membrane-proximal Amino Acids Of the Cytoplasmic Tail Ofmentioning

confidence: 91%

“…For example, the transferrin receptor (TfR), which like SR-A, is a type II transmembrane receptor, has a well defined cytoplasmic motif (YTRF) that is required for receptor internalization (15). Previous studies with SR-A have identified specific amino acids in the cytoplasmic tail that are involved in regulating receptor internalization and cell-surface expression (13,16,17). However, the importance of cytoplasmic domains in SR-Amediated adhesion has not been addressed.…”

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confidence: 99%

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Class A Scavenger Receptor-mediated Adhesion and Internalization Require Distinct Cytoplasmic Domains

Kosswig

Rice

Daugherty

et al. 2003

Journal of Biological Chemistry

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“…However, consensus recognition sequences for protein kinase C isoforms (Thr-10), casein kinase II (Ser-18), and potential phosphorylation at five serine residues (Ser-18, Ser-28, Ser-30, Ser-54, and Ser-56) and a single threonine (Thr-10) were predicted. It may be relevant that a block of five amino acids beginning at Phe-24 is highly conserved with SR-A1 I/II, and mutagenesis of the bovine molecule has demonstrated that the residues Phe-24 and Asp-25 are important for efficient internalization and cell surface expression of the receptor (30).…”

Section: Identification and Predicted Domain Organization Of The Clasmentioning

confidence: 99%

Identification and Characterization of Murine SCARA5, a Novel Class A Scavenger Receptor That Is Expressed by Populations of Epithelial Cells

Jiang

Oliver

Davies

et al. 2006

Journal of Biological Chemistry

135

119

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Epithelia are positioned at a critical interface to prevent invasion by microorganisms from the environment. Pattern recognition receptors are important components of innate immunity because of their ability to interact with specific microbe-associated structures and initiate immune responses. Several distinct groups of receptors have been recognized. One of these, the scavenger receptors, has been classified into at least eight separate classes. The class A scavenger receptors are characterized by the presence of a collagen-like domain and include macrophage scavenger receptor type A (SR-A1 I/II, SCARA1) and MARCO (SCARA2). These receptors are known to make important contributions to host defense. Here, we identify a novel murine scavenger receptor, SCARA5, which has a structure typical of this class. The cDNA encodes 491 amino acids, which predict a type II protein that contains C-terminal intracellular, transmembrane, extracellular spacer, collagenous, and N-terminal scavenger receptor cysteine rich domains. Expression in Chinese hamster ovary cells confirmed that the receptor assembles as a homotrimer and is expressed at the plasma membrane. SCARA5-transfected cells bound Escherichia coli and Staphylococcus aureus, but not zymosan, in a polyanionic-inhibitable manner. Unlike other class A scavenger receptors, the receptor was unable to endocytose acetylated or oxidized low density lipoprotein. Quantitative RT-PCR and in situ hybridization demonstrate SCARA5 has a tissue and cellular distribution unique among class A scavenger receptors. Because of the restriction of SCARA5 transcripts to populations of epithelial cells, we propose that this receptor may play important roles in the innate immune activities of these cells.Mucosal surfaces are the predominant route of microbial entry into the host. Epithelial cells that line mucosa not only form a mechanical barrier that pathogens must overcome to invade the underlying tissues but also make specific contributions to the initiation of mucosal inflammation and associated immune responses (1). Although the immunological activities of epithelia have been under-investigated with comparison to those of hematopoietic cells, an increasing number of studies has given weight to the proposal that they are an active component of the innate immune system. The evidence is that epithelia such as those of the airway and urinary and intestinal tracts can sense microbes and signal their presence to cells of the underlying mucosa to activate appropriate anti-microbial and immunological responses (2). Recent demonstrations have shown that epithelial cells can themselves produce cytokines, chemokines, and other effector molecules following contact with bacteria and thus both influence and augment the immune response (3-5).Cells of the innate immune system have evolved a number of germ line-encoded receptors, termed pattern recognition receptors (PRRs), 4 which they employ to discriminate microbial cells from those of the host (6). PRRs are evolutionary ancient and have been highly ...

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VXFD in the Cytoplasmic Domain of Macrophage Scavenger Receptors Mediates Their Efficient Internalization and Cell-Surface Expression.

Cited by 21 publications

References 0 publications

The Microtubule-binding Protein Hook3 Interacts with a Cytoplasmic Domain of Scavenger Receptor A

The Microtubule-binding Protein Hook3 Interacts with a Cytoplasmic Domain of Scavenger Receptor A

Class A Scavenger Receptor-mediated Adhesion and Internalization Require Distinct Cytoplasmic Domains

Identification and Characterization of Murine SCARA5, a Novel Class A Scavenger Receptor That Is Expressed by Populations of Epithelial Cells

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