ArticleCellular and molecular life sciences : CMLS2019
Protein interacting with Amyloid Precursor Protein tail-1 (PAT1) is involved in early endocytosis.
Article in Cellular and molecular life sciences : CMLS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- De novo variants in DENND5B cause a neurodevelopmental disorder.American journal of human genetics · 2024Article
- Receptor-mediated internalization promotes increased endosome size and number in a RAB4- and RAB5-dependent manner.European journal of cell biology · 2023Article
- AP2S1 regulates APP degradation through late endosome-lysosome fusion in cells and APP/PS1 mice.Traffic (Copenhagen, Denmark) · 2023Article
- The Rabep1-Mediated Endocytosis and Activation of Trypsinogen to Promote Pancreatic Stellate Cell Activation.Biomolecules · 2022Article
- The Rab5 activator RME-6 is required for amyloid precursor protein endocytosis depending on the YTSI motif.Cellular and molecular life sciences : CMLS · 2020Article
- The Drosophila amyloid precursor protein homologue mediates neuronal survival and neuroglial interactions.PLoS biology · 2020Article
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Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
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Abstract
Protein interacting with Amyloid Precursor Protein (APP) tail 1 (PAT1) also called APPBP2 or Ara 67 has different targets such as APP or androgen receptor and is expressed in several tissues. PAT1 is known to be involved in the subcellular trafficking of its targets. We previously observed in primary neurons that PAT1 is poorly associated with APP at the cell surface. Here we show that PAT1 colocalizes with vesicles close to the cell surface labeled with Rab5, Rab4, EEA1 and Rabaptin-5 but not with Rab11 and Rab7. Moreover, PAT1 expression regulates the number of EEA1 and Rab5 vesicles, and endocytosis/recycling of the transferrin receptor. In addition, low levels of PAT1 decrease the size of transferrin-colocalized EEA1 vesicles with time following transferrin uptake. Finally, overexpression of the APP binding domain to PAT1 is sufficient to compromise endocytosis. Altogether, these data suggest that PAT1 is a new actor in transferrin early endocytosis. Whether this new function of PAT1 may have consequences in pathology remains to be determined.
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