Analysis of conserved residues in the betapat-3 cytoplasmic tail reveals important functions of integrin in multiple tissues.
Integrin cytoplasmic tails contain motifs that link extracellular information to cell behavior such as cell migration and contraction. To investigate the cell functions mediated by the conserved motifs, we created mutations in the Caenorhabditis elegans betapat-3 cytoplasmic tail. The beta1D (799FK800), NPXY, tryptophan (784W), and threonine (797TT798) motifs were disrupted to identify their functions in vivo. Animals expressing integrins with disrupted NPXY motifs were viable, but displayed distal tip cell migration and ovulation defects. The conserved threonines were required for gonad migration and contraction as well as tail morphogenesis, whereas disruption of the beta1D and tryptophan motifs produced only mild defects. To abolish multiple conserved motifs, a beta1C-like variant, which results in a frameshift, was constructed. The betapat-3(beta1C) transgenic animals showed cold-sensitive larval arrests and defective muscle structure and gonad migration and contraction. Our study suggests that the conserved NPXY and TT motifs play important roles in the tissue-specific function of integrin.
Xu
Xiaojian
X
Department of Biology, Baylor University, Waco, Texas, USA.
Ahn
Jeong H
JH
Tam
Phebe
P
Yu
Eun Jeong
EJ
Batra
Sushil
S
Cram
Erin J
EJ
Lee
Myeongwoo
M
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans; D003593:Cytoplasm / Q000378:metabolism*; D005260:Female; D006801:Humans; D019012:Integrin beta1 / Q000378:metabolism; D016023:Integrins / Q000378:metabolism*; D008969:Molecular Sequence Data; D010060:Ovulation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013912:Threonine / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry
D019012:Integrin beta1; D016023:Integrins; C403487:integrin beta1C; D013912:Threonine; D014443:Tyrosine