ArticleCellular and molecular life sciences : CMLS2009
HIP1 exhibits an early recruitment and a late stage function in the maturation of coated pits.
Article in Cellular and molecular life sciences : CMLS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Abnormally high HIP1 expression is associated with metastatic behaviors and poor prognosis in ESCC.Oncology letters · 2021Article
- Functional characterization of 67 endocytic accessory proteins using multiparametric quantitative analysis of CCP dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Huntingtin-interacting protein family members have a conserved pro-viral function fromProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Endocytic pathways involved in filovirus entry: advances, implications and future directions.Viruses · 2012Review
- Article
- Differential requirements for clathrin endocytic pathway components in cellular entry by Ebola and Marburg glycoprotein pseudovirions.Virology · 2011Article
- Quantitative analysis of endocytosis with cytoplasmic pHluorin chimeras.Traffic (Copenhagen, Denmark) · 2010Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
Huntingtin interacting protein 1 (HIP1) is an accessory protein of the clathrin-mediated endocytosis (CME) pathway, yet its precise role and the step at which it becomes involved are unclear. We employed live-cell imaging techniques to focus on the early steps of CME and characterize HIP1 dynamics. We show that HIP1 is highly colocalized with clathrin at the plasma membrane and shares similar dynamics with a subpopulation of clathrin assemblies. Employing transferrin receptor fused to pHluorin, we distinguished between open pits to which HIP1 localizes and newly internalized vesicles that are devoid of HIP1. Moreover, shRNA knockdown of clathrin compromised HIP1 membranal localization, unlike the reported behavior of Sla2p. HIP1 fragment, lacking its ANTH and Talin-like domains, inhibits internalization of transferrin, but retains colocalization with membranal clathrin assemblies. These data demonstrate HIP1's role in pits maturation and formation of the coated vesicle, and its strong dependence on clathrin for membranal localization.
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