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Publication

Targeted disruption of cubilin reveals essential developmental roles in the structure and function of endoderm and in somite formation.

Brian T Smith | Jason C Mussell | Paul A Fleming | Jeremy L Barth | Demetri D Spyropoulos | Marion A Cooley | Christopher J Drake | W Scott Argraves
BMC developmental biology | 2006

Cubilin is a peripheral membrane protein that interacts with the integral membrane proteins megalin and amnionless to mediate ligand endocytosis by absorptive epithelia such as the extraembryonic visceral endoderm (VE).

Pubmed ID: 16787536

Research resources used in this publication

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Associated grants

  • Agency: NHLBI NIH HHS, United States
    Id: HL061873
  • Agency: NHLBI NIH HHS, United States
    Id: T32 HL07260
  • Agency: NCI NIH HHS, United States
    Id: R03 CA109958
  • Agency: NHLBI NIH HHS, United States
    Id: HL57375
  • Agency: NIDCR NIH HHS, United States
    Id: DE14347
  • Agency: NHLBI NIH HHS, United States
    Id: R01 HL061873
  • Agency: NHLBI NIH HHS, United States
    Id: T32 HL007710
  • Agency: NIDCR NIH HHS, United States
    Id: R01 DE014347
  • Agency: NCI NIH HHS, United States
    Id: CA109958
  • Agency: NHLBI NIH HHS, United States
    Id: R01 HL057375
  • Agency: NHLBI NIH HHS, United States
    Id: T32 HL007260

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C57BL/6J (tool)

RRID:IMSR_JAX:000664

Mus musculus with name C57BL/6J from IMSR.

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