Nuestro grupo organiza más de 3000 Series de conferencias Eventos cada año en EE. UU., Europa y América. Asia con el apoyo de 1.000 sociedades científicas más y publica más de 700 Acceso abierto Revistas que contienen más de 50.000 personalidades eminentes, científicos de renombre como miembros del consejo editorial.

Revistas de acceso abierto que ganan más lectores y citas
700 revistas y 15 000 000 de lectores Cada revista obtiene más de 25 000 lectores

Abstracto

A GFP Retinal Prion Proteins Intracellular Trafficking via Endocytic Intermediates

Tarunkanti Mondal

The prion protein (PrP) is a key molecule implicated in neurodegenerative disorders. Understanding its intracellular trafficking is essential for unraveling its physiological and pathological functions. This article focuses on the intracellular trafficking of a green fluorescent protein (GFP) tagged PrP in retinal cells, specifically exploring its transport via endocytic intermediates. Endocytic pathways, including clathrin-mediated endocytosis, caveolaemediated endocytosis, and macropinocytosis, play a crucial role in PrP internalization and trafficking. Endocytic intermediates, such as early endosomes, late endosomes, and lysosomes, are involved in sorting, recycling, and degradation of endocytosed proteins. Live-cell imaging and colocalization studies have provided insights into GFPPrP’s movement and localization within these organelles. Studies reveal rapid internalization of PrP via clathrinmediated endocytosis, with subsequent transport to early endosomes. A fraction of PrP is recycled, while the remainder progresses to late endosomes and lysosomes for degradation. Elucidating the intracellular trafficking of GFP-PrP and its association with endocytic intermediates enhances our understanding of PrP’s functions and implications in neurodegenerative diseases. Further investigations are needed to explore the molecular machinery involved and the impact of disease-associated mutations. This knowledge may contribute to potential therapeutic strategies for prion diseases.