Evolution of Integrin I Domains

Johnson, Mark S.; Chouhan, Bhanupratap Singh

doi:10.1007/978-94-017-9153-3_1

Cited by 15 publications

(15 citation statements)

References 100 publications

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“…However, further inspection of the cartilaginous fish genome sheds little direct light: the ghost shark contains orthologues of α1β1, α2β1 and α11β1, but appears to lack α10 [37], confirmed here using each human integrin sequence to search the C. milii genome. These shark integrins all contain the critical, permissive, Glu residue, so that they are predicted to bind Site 1 in collagens I and III.…”

Section: Discussionmentioning

confidence: 85%

Unique charge-dependent constraint on collagen recognition by integrin α10β1

et al. 2017

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The collagen-binding integrins recognise collagen through their inserted (I) domain, where co-ordination of a Mg2 + ion in the metal ion-dependent site is reorganised by ligation by a collagen glutamate residue found in specific collagen hexapeptide motifs. Here we show that GROGER, found in the N-terminal domain of collagens I and III, is only weakly recognised by α10β1, an important collagen receptor on chondrocytes, contrasting with the other collagen-binding integrins. Alignment of I domain sequence and molecular modelling revealed a clash between a unique arginine residue (R215) in α10β1 and the positively-charged GROGER. Replacement of R215 with glutamine restored binding. Substituting arginine at the equivalent locus (Q214) in integrins α1 and α2 I domains impaired their binding to GROGER. Collagen II, abundant in cartilage, lacks GROGER. GRSGET is uniquely expressed in the C-terminus of collagen II, but this motif is similarly not recognised by α10β1. These data suggest an evolutionary imperative to maintain accessibility of the terminal domains of collagen II in tissues such as cartilage, perhaps during endochondral ossification, where α10β1 is the main collagen-binding integrin.

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Section: Discussionmentioning

confidence: 85%

Unique charge-dependent constraint on collagen recognition by integrin α10β1

et al. 2017

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“…Here we use a genome-wide screening for α/β integrins in the oyster. Although oyster integrins display more structural variability, such as FA-GAP region, sulfotransferase domain in α integrin proteins, and extra INB (or βI) domain in β integrin proteins, they all contain conserved domains, including the extracellular INA domain, Intα domain in the α integrin proteins, or extracellular INB domain in the β integrin proteins, and a short transmembrane domain and cytoplasmic domain in both α and β integrin proteins, as most integrins in other species (10,65). Multiple sequence alignments of oyster integrins also reveals that seven of eight α integrin proteins and two of three β integrin proteins harbor the conserved motifs of GFFXR and NPX[Y/F] in their cytoplasmic region.…”

Section: Discussionmentioning

confidence: 99%

The Members of the Highly Diverse Crassostrea gigas Integrin Family Cooperate for the Generation of Various Immune Responses

Qiu

Wang

et al. 2020

Front. Immunol.

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Studies on invertebrate immune receptors can provide insights into characteristics specific to innate immune system. Here, eight α and three β integrins are identified from an invertebrate, the Pacific oyster Crassostrea gigas, and their possible immune functions are studied. Oyster α/β integrins exhibit a higher degree of sequence and structural variability than the members from Homo sapiens and Drosophila melanogaster. The analysis reveals that oyster RGD-and laminin-binding receptor homologs are present in the phylogenetic tree of α integrins, but the other six oyster α integrins mainly form a species-specific branch; meanwhile, oyster β integrins are clustered with insect β integrins but distinct from a member from the mollusk Biomphalaria glabrata. Although phylogenetically lacking the important α integrin branches of LDV-binding, PS3-type, and αI-containing integrins, oyster integrins can bind to most ECM ligands, including RGDCP, LDVCP, GFOGERCP, and laminin protein in a distinct binding pattern. Besides, oyster integrins are distributed in different hemocyte subpopulations, while only specific integrins are selectively involved in hemocyte phagocytosis, migration, and encapsulation, and some of them participate in more than one immune response in a sophisticated pattern. Especially, oyster β integrins are arranged in the core to mediate complex immune responses, unlike the counterparts in humans that mainly depend on αI-containing integrins to incite immune reactions. This study represents the first comprehensive attempt to reveal the structural and evolutionary features of the integrin family and their involvement in cellular immune responses in the non-model invertebrate C. gigas and sheds light on the characteristics specific to the innate immune system in the integrin family.

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“…Integrins are essential for regulation of numerous cellular functions including cell signaling and adhesion. Nine of the eighteen integrin alpha subunits harbor a conserved I (inserted)-domain that is crucial for binding of endogenous ligands ( Johnson and Chouhan, 2014 ). Four of these integrin alpha subunits (α D , α L , α M and α X ) form heterodimers exclusively with the β 2 subunit, thus forming the α D β 2 (CD11d/CD18), α L β 2 (CD11a/CD18, LFA-1), α M β 2 (CD11b/CD18, complement receptor 3 (CR3), Mac1) and α X β 2 (CD11c/CD18, CR4, p150/195) integrins, respectively ( Arnaout, 1990 ; Mazzone and Ricevuti, 1995 ; Sanchez-Madrid, 1983 ; Tan, 2012 ; Van der Vieren et al, 1995 ).…”

Section: Introductionmentioning

confidence: 99%

Bordetella adenylate cyclase toxin is a unique ligand of the integrin complement receptor 3

Osička

Osičková

Hasan

et al. 2015

eLife

123

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Integrins are heterodimeric cell surface adhesion and signaling receptors that are essential for metazoan existence. Some integrins contain an I-domain that is a major ligand binding site. The ligands preferentially engage the active forms of the integrins and trigger signaling cascades that alter numerous cell functions. Here we found that the adenylate cyclase toxin (CyaA), a key virulence factor of the whooping cough agent Bordetella pertussis, preferentially binds an inactive form of the integrin complement receptor 3 (CR3), using a site outside of its I-domain. CyaA binding did not trigger downstream signaling of CR3 in human monocytes and CyaA-catalyzed elevation of cAMP effectively blocked CR3 signaling initiated by a natural ligand. This unprecedented type of integrin-ligand interaction distinguishes CyaA from all other known ligands of the I-domain-containing integrins and provides a mechanistic insight into the previously observed central role of CyaA in the pathogenesis of B. pertussis.DOI: http://dx.doi.org/10.7554/eLife.10766.001

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Evolution of Integrin I Domains

Cited by 15 publications

References 100 publications

Unique charge-dependent constraint on collagen recognition by integrin α10β1

Unique charge-dependent constraint on collagen recognition by integrin α10β1

The Members of the Highly Diverse Crassostrea gigas Integrin Family Cooperate for the Generation of Various Immune Responses

Bordetella adenylate cyclase toxin is a unique ligand of the integrin complement receptor 3

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