Complete amino acid sequence of a novel integrin beta subunit (beta 6) identified in epithelial cells using the polymerase chain reaction.

Sheppard, Dean; Rozzo, Carla; Starr, Lisa; Quaranta, Vito; Erle, David J.; Pytela, Robert

doi:10.1016/s0021-9258(19)38425-x

Cited by 174 publications

(26 citation statements)

References 18 publications

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“…CS-1 cells expressing etv133 composed of [~3.762 (wild-type) or 133.751 eral integrin 13 subunit cytoplasmic tails. The deduced amino acid sequences of the 13 subunit cytoplasmic tails listed above are obtained from the following published data: 131 (Argraves et al, 1987), 132 (Kishimoto et al, 1987), 133 (Fitzgerald et al, 1987), 1~5 (McLean et al, 1990, 66 (Sheppard et al, 1990), and 137 (Erie et al, 1991). For each 13 subunit, the first amino acid listed is the residue that follows the transmembrane anchor.…”

Section: Residues 742-751 Within the F13 Cytoplasmic Tail Are Required For Av133-dependent Cellular Adhesion And Spreadingmentioning

confidence: 99%

Requirement of the NPXY motif in the integrin beta 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo.

Filardo

Brooks

Deming

et al. 1995

The Journal of Cell Biology

181

138

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Abstract. The NPXY sequence is highly conserved among integrin 13 subunit cytoplasmic tails, suggesting that it plays a fundamental role in regulating integrinmediated function. Evidence is provided that the NPXY structural motif within the 133 subunit, comprising residues 744-747, is essential for cell morphological and migratory responses mediated by integrin av133 in vitro and in vivo. Transfection of CS-1 melanoma cells with a cDNA encoding the wild-type integrin 133 subunit, results in de novo e~v133 expression and cell attachment, spreading, and migration on vitronectin. CS-1 cells expressing t~v133 with mutations that disrupt the NPXY sequence interact with soluble vitronectin or an RGD peptide, yet fail to attach, spread, or migrate on immobilized ligand. The biological consequences of these observations are underscored by the finding that CS-1 cells expressing wild-type o~v133 acquire the capacity to form spontaneous pulmonary metastases in the chick embryo when grown on the chorioallantoic membrane. However, migration-deficient CS-1 cells expressing av[33 with mutations in the NPXY sequence lose this ability to metastasize. These findings demonstrate that the NPXY motif within the integrin 133 cytoplasmic tail is essential for uv133-dependent postligand binding events involved in cell migration and the metastatic phenotype of melanoma cells.C ELL adhesion and migration play a central role in diverse biological and pathological processes including embryogenesis, angiogenesis, wound healing, and metastasis. Although the mechanisms that regulate cell adhesion and motility are poorly understood, it is clear that in many instances, these events are initiated by the specific recognition of extracellular matrix proteins by a family of cell surface adhesion receptors known as integrins (Ruoslahti, 1991;Hynes, 1992). Upon ligand recognition, integrins typically cluster at the site of ceU-substrate interface; this leads to polymerization of the actin cytoskeleton (Burridge et al., 1988). In this context, integrins form a physical linkage between the extracellular matrix and the actin cytoskeleton. Ultimately, these integrin-initiated adhesive interactions can lead to gross changes in cellular morphology orchestrated by the actin cytoskeleton that facilitate cell migration.Structurally, integrins are heterodimers composed of noncovalently associated a and [3 subunits (Hynes, 1992 554-8926. which in most cases is shorter than 50 amino acids. Although several studies have identified functionally important regions within the integrin ectodomain Cheresh, 1988, 1990;D'Souza et al., 1988D'Souza et al., , 1990D'Souza et al., , 1994Loftus et al., 1990;Takada et al., 1992;Lee et al., 1995) and cytoplasmic domain (Hibbs et al., 1991;O'Toole et al., 1991O'Toole et al., , 1995Bauer et al., 1993;Filardo and Cheresh, 1994) that can regulate ligand-binding function, relatively little is known regarding structural motifs within the integrin that regulate morphological changes in cell shape which accompany cellular adhesion...

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Section: Residues 742-751 Within the F13 Cytoplasmic Tail Are Required For Av133-dependent Cellular Adhesion And Spreadingmentioning

confidence: 99%

Requirement of the NPXY motif in the integrin beta 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo.

Filardo

Brooks

Deming

et al. 1995

The Journal of Cell Biology

181

138

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“…Numbering for B1 is for the chicken sequence; the human sequence is identical in the region shown but the corresponding number is 783. Sequence references: B2 (43), B1(31,44), B3(45), B5(34,35), B6(46), ~7(47), and B4 (48, 49).…”

mentioning

confidence: 99%

The cytoplasmic domain of the integrin lymphocyte function-associated antigen 1 beta subunit: sites required for binding to intercellular adhesion molecule 1 and the phorbol ester-stimulated phosphorylation site.

Hibbs

Jakes

Stacker

et al. 1991

The Journal of Experimental Medicine

225

136

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SummaryWe have defined the regions of the cytoplasmic domain of the leukocyte integrin lymphocyte function-associated antigen 1 (LFA-1) that are required for active binding of its extracellular domain to intercellular adhesion molecule 1 (ICAM-1). The NH2-terminal 28 amino acids in the cytoplasmic domain are dispensable, but a segment of 5 amino acids including three contiguous threonines (758-760) and Phe 766 in the COOH-terminal third of the cytoplasmic domain are required for binding to ICAM-1. Mutation and phosphoamino acid analysis show that Set 756 is the major residue phosphorylated in response to phorbol ester. Furthermore, multiple mutations demonstrate that serine phosphorylation can be dissociated from phorbol ester-stimulated binding of LFA-1 to ICAM-1. The sites we have defined are previously unremarked, are well conserved in the ~31, 133, and B7 integrin subunits, and may be of broad importance in regulating adhesiveness of integrins.

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“…Cloning and sequencing of ovine integrin-b 6 subunit (Figure 1) revealed close homology (z88%) with its human counterpart (Sheppard et al 1990), which has previously been shown to convey susceptibility to FMDV infection when expressed in the normally nonpermissive cell line SW480 (Jackson et al 2000).…”

Section: Discussionmentioning

confidence: 88%

Integrin-α_vβ₆, a Putative Receptor for Foot-and-Mouth Disease Virus, Is Constitutively Expressed in Ruminant Airways

Brown

McALEESE²,

Thornton³

et al. 2006

J Histochem Cytochem.

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Evolved functions of integrin-αvβ6 include roles in epithelial cell-extracellular matrix protein interactions and in the binding and activation of latent TGF-β1. Integrin-αvβ6 is also exploited as a receptor by foot-and-mouth disease virus (FMDV) and may play a significant role in its transmission and pathogenesis. The ovine β6 integrin subunit was cloned and sequenced (EMBL accession no. AJ439062). Screening of normal ovine tissues by RT-PCR and immunocytochemistry confirmed that integrin-αvβ6 is restricted to sheep epithelial cells. Integrin-αvβ6 expression was detected in epithelia of the airways, oral cavity, gastrointestinal tract, kidney, sweat glands, hair follicle sheaths, and the epidermis of pedal coronary band (PB) but not of normal skin. Consistent with FMDV tropism, integrin-αvβ6 was detected within the basal layers of the stratified squamous epithelium of the oral mucosa and PB. In addition, integrin-αvβ6 appears to be constitutively expressed in the normal airways of both cattle and sheep. The latter finding suggests that ruminant airway epithelium presents a highly accessible target for initiation of infection with FMDV by inhalation.

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Complete amino acid sequence of a novel integrin beta subunit (beta 6) identified in epithelial cells using the polymerase chain reaction.

Cited by 174 publications

References 18 publications

Requirement of the NPXY motif in the integrin beta 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo.

Requirement of the NPXY motif in the integrin beta 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo.

The cytoplasmic domain of the integrin lymphocyte function-associated antigen 1 beta subunit: sites required for binding to intercellular adhesion molecule 1 and the phorbol ester-stimulated phosphorylation site.

Integrin-α_vβ₆, a Putative Receptor for Foot-and-Mouth Disease Virus, Is Constitutively Expressed in Ruminant Airways

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Complete amino acid sequence of a novel integrin beta subunit (beta 6) identified in epithelial cells using the polymerase chain reaction.

Cited by 174 publications

References 18 publications

Requirement of the NPXY motif in the integrin beta 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo.

Requirement of the NPXY motif in the integrin beta 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo.

The cytoplasmic domain of the integrin lymphocyte function-associated antigen 1 beta subunit: sites required for binding to intercellular adhesion molecule 1 and the phorbol ester-stimulated phosphorylation site.

Integrin-αvβ6, a Putative Receptor for Foot-and-Mouth Disease Virus, Is Constitutively Expressed in Ruminant Airways

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Integrin-α_vβ₆, a Putative Receptor for Foot-and-Mouth Disease Virus, Is Constitutively Expressed in Ruminant Airways