Receptor-mediated cellular entry of nuclear localizing anti-DNA antibodies via myosin 1

Kumiko Yanase, Robert M. Smith, Antonio Puccetti, Leonard Jarett, Michael P. Madaio

Research output: Contribution to journalArticlepeer-review

134 Scopus citations


A unique subset of anti-DNA antibodies enters living cells, interacts with DNase 1, and inhibits endonuclease activity, before their nuclear localization and subsequent attenuation of apoptosis. We now report that endocytosis of these immunoglobulins is mediated by cell surface binding to brush border myosin (myosin 1). Cellular entry and internalization via this unique receptor provides initial contact for entry and sorting these immunoglobulins to translocate to the nuclear pore and enter the nucleus, interact with DNase 1 within the cytoplasm, or recycle back to the cell surface. This internalization pathway provides clues to the translocation of large proteins across cell membranes and the functional effects of intracellular antibodies on cytopathology. This is the first demonstration that brush border myosin functions as a specific cell surface receptor for internalization of large proteins.

Original languageEnglish (US)
Pages (from-to)25-31
Number of pages7
JournalJournal of Clinical Investigation
Issue number1
StatePublished - Jul 1 1997
Externally publishedYes


  • Autoantibody
  • Autoimmunity
  • Cell surface receptor
  • Endocytosis
  • Systemic lupus erythematosus

ASJC Scopus subject areas

  • Medicine(all)


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