The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement

Shasta L. Sabo, Annat F. Ikin, Joseph D. Buxbaum, Paul Greengard

Research output: Contribution to journalArticlepeer-review

191 Scopus citations

Abstract

FE65 binds to the Alzheimer amyloid precursor protein (APP), but the function of this interaction has not been identified. Here, we report that APP and FE65 are involved in regulation of cell movement. APP and FE65 colocalize with actin and Mena, an Ab1-associated signaling protein thought to regulate actin dynamics, in lamellipodia. APP and FE65 specifically concentrate with β1-integrin in dynamic adhesion sites known as focal complexes, but not in more static adhesion sites known as focal adhesions. Overexpression of APP accelerates cell migration in an MDCK cell wound-healing assay. Coexpression of APP and FE65 dramatically enhances the effect of APP on cell movement, probably by regulating the amount of APP at the cell surface. These data are consistent with a role for FE65 and APP, possibly in a Mena-containing macromolecular complex, in regulation of actin-based motility.

Original languageEnglish
Pages (from-to)1403-1414
Number of pages12
JournalJournal of Cell Biology
Volume153
Issue number7
DOIs
StatePublished - Jun 26 2001

Keywords

  • Adhesion
  • Amyloid precursor protein
  • Cell movement
  • FE65
  • Mena

Fingerprint

Dive into the research topics of 'The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement'. Together they form a unique fingerprint.

Cite this