ß1B Integrin interferes with matrix assembly but not with confluent monolayer polarity, and alters some morphogenetic properties of FRT epithelial cells

Calı̀, Gaetano; Retta, Saverio Francesco; Negri, Rosa; Damiano, Ivana; Gentile, Raffaele; Tarone, Guido; Nitsch, Lucio; Garbi, Corrado

doi:10.1016/s0171-9335(98)80053-8

Cited by 12 publications

(16 citation statements)

References 68 publications

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“…The ␤1B isoform is expressed primarily in skin and liver, where it constitutes a minority of the ␤1 protein (Balzac et al, 1993). To date, no function of ␤1B has been demonstrated in situ, but there have been a number of studies of the properties of the isoform in cultured cells (Balzac et al, 1993(Balzac et al, , 1994Cali et al, 1998;Retta et al, 1998;Armulik et al, 2000). Overall, this work indicates that ␤1B is deficient in both "outside in" and "inside out" integrin signaling.…”

Section: Similarity To Mammalian ␤ Subunit Variantsmentioning

confidence: 76%

Disruption of C-Terminal Cytoplasmic Domain of βPS Integrin Subunit Has Dominant Negative Properties in DevelopingDrosophila

Jannuzi

Bunch

Brabant

et al. 2002

MBoC

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We have analyzed a set of new and existing strong mutations in the myospheroid gene, which encodes the betaPS integrin subunit of Drosophila. In addition to missense and other null mutations, three mutants behave as antimorphic alleles, indicative of dominant negative properties. Unlike null alleles, the three antimorphic mutants are synthetically lethal in double heterozygotes with an inflated (alphaPS2) null allele, and they fail to complement very weak, otherwise viable alleles of myospheroid. Two of the antimorphs result from identical splice site lesions, which create a frameshift in the C-terminal half of the cytoplasmic domain of betaPS. The third antimorphic mutation is caused by a stop codon just before the cytoplasmic splice site. These mutant betaPS proteins can support cell spreading in culture, especially under conditions that appear to promote integrin activation. Analyses of developing animals indicate that the dominant negative properties are not a result of inefficient surface expression, or simple competition between functional and nonfunctional proteins. These data indicate that mutations disrupting the C-terminal cytoplasmic domain of integrin beta subunits can have dominant negative effects in situ, at normal levels of expression, and that this property does not necessarily depend on a specific new protein sequence or structure. The results are discussed with respect to similar vertebrate beta subunit cytoplasmic mutations.

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Section: Similarity To Mammalian ␤ Subunit Variantsmentioning

confidence: 76%

Disruption of C-Terminal Cytoplasmic Domain of βPS Integrin Subunit Has Dominant Negative Properties in DevelopingDrosophila

Jannuzi

Bunch

Brabant

et al. 2002

MBoC

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“…In particular, we have shown that the unique cytoplasmic sequences of ␤ 1 B and ␤ 1 D endow these molecules with distinctive functional properties with respect to a number of cellular functions (Balzac et al, 1994;Belkin et al, 1997;Belkin and Retta, 1998;Calì et al, 1998;Retta et al, 1998). In particular, we have shown that the unique cytoplasmic sequences of ␤ 1 B and ␤ 1 D endow these molecules with distinctive functional properties with respect to a number of cellular functions (Balzac et al, 1994;Belkin et al, 1997;Belkin and Retta, 1998;Calì et al, 1998;Retta et al, 1998).…”

Section: ␤ 1 Effect Over ␣ V Integrins Occurs Irrespective Of the Typmentioning

confidence: 88%

Cross Talk between β₁and α_VIntegrins: β₁Affects β₃mRNA Stability

Retta

Cassarà

D'Amato

et al. 2001

MBoC

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There is increasing evidence that a fine-tuned integrin cross talk can generate a high degree of specificity in cell adhesion, suggesting that spatially and temporally coordinated expression and activation of integrins are more important for regulated cell adhesive functions than the intrinsic specificity of individual receptors. However, little is known concerning the molecular mechanisms of integrin cross talk. With the use of beta(1)-null GD25 cells ectopically expressing the beta(1)A integrin subunit, we provide evidence for the existence of a cross talk between beta(1) and alpha(V) integrins that affects the ratio of alpha(V)beta(3) and alpha(V)beta(5) integrin cell surface levels. In particular, we demonstrate that a down-regulation of alpha(V)beta(3) and an up-regulation of alpha(V)beta(5) occur as a consequence of beta(1)A expression. Moreover, with the use of GD25 cells expressing the integrin isoforms beta(1)B and beta(1)D, as well as two beta(1) cytoplasmic domain deletion mutants lacking either the entire cytoplasmic domain (beta(1)TR) or only its "variable" region (beta(1)COM), we show that the effects of beta(1) over alpha(V) integrins take place irrespective of the type of beta(1) isoform, but require the presence of the "common" region of the beta(1) cytoplasmic domain. In an attempt to establish the regulatory mechanism(s) whereby beta(1) integrins exert their trans-acting functions, we have found that the down-regulation of alpha(V)beta(3) is due to a decreased beta(3) subunit mRNA stability, whereas the up-regulation of alpha(V)beta(5) is mainly due to translational or posttranslational events. These findings provide the first evidence for an integrin cross talk based on the regulation of mRNA stability.

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“…We used the mouse NIH/3T3 (ATCC CRL-1658), GD25 , sEnd.1 (Williams et al, 1988) and N1E-115 (ATCC CRL-2263), the human HEK293 (ATCC CRL-1573), MCF10A (ATCC CRL-10317), T-47D (ATCC HTB-133) and ECV-304 (ATCC CRL-1998), the monkey COS7 (ATCC CRL-1651), and the rat FRT (Cali et al, 1998) cell lines. All cell lines were cultured in Dulbecco's modified Eagle's medium (DMEM), containing 10% foetal calf serum (FCS), 2 mM glutamine and penicillin/streptomycin (50 IU/ ml, 50 mg/ml), except FRT, T-47D and MCF10A cells cultured in Coon's F12, RPMI 1640 and MEGM medium, respectively.…”

Section: Cell Lines and Tissuesmentioning

confidence: 99%

Identification of Krit1B: a novel alternative splicing isoform of cerebral cavernous malformation gene-1

Retta

Avolio

Francalanci

et al. 2004

Gene

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ß1B Integrin interferes with matrix assembly but not with confluent monolayer polarity, and alters some morphogenetic properties of FRT epithelial cells

Cited by 12 publications

References 68 publications

Disruption of C-Terminal Cytoplasmic Domain of βPS Integrin Subunit Has Dominant Negative Properties in DevelopingDrosophila

Disruption of C-Terminal Cytoplasmic Domain of βPS Integrin Subunit Has Dominant Negative Properties in DevelopingDrosophila

Cross Talk between β₁and α_VIntegrins: β₁Affects β₃mRNA Stability

Identification of Krit1B: a novel alternative splicing isoform of cerebral cavernous malformation gene-1

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ß1B Integrin interferes with matrix assembly but not with confluent monolayer polarity, and alters some morphogenetic properties of FRT epithelial cells

Cited by 12 publications

References 68 publications

Disruption of C-Terminal Cytoplasmic Domain of βPS Integrin Subunit Has Dominant Negative Properties in DevelopingDrosophila

Disruption of C-Terminal Cytoplasmic Domain of βPS Integrin Subunit Has Dominant Negative Properties in DevelopingDrosophila

Cross Talk between β1and αVIntegrins: β1Affects β3mRNA Stability

Identification of Krit1B: a novel alternative splicing isoform of cerebral cavernous malformation gene-1

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Cross Talk between β₁and α_VIntegrins: β₁Affects β₃mRNA Stability