title: Autophagy receptor defects and ALS-FTLD.
abstract: Various pathophysiological mechanisms have been implicated in the ALS-FTLD clinicopathological spectrum of neurodegenerative disorders. Here we focus on the role of autophagy, an intracellular catabolic pathway, in these conditions. Growing evidence suggests that the autophagic process can be disturbed in ALS-FTLD, including by genetic mutations affecting autophagy receptor proteins (ubiquilin-2, optineurin, SQSTM1/p62) and regulators (VCP). Such mutations may impair clearance of autophagy substrates with pathological consequences. Recent studies have also uncovered a direct connection between autophagy and RNA processing, supporting an integrated model connecting several ALS-FTLD associated gene products. This article is part of a Special Issue entitled 'Neuronal Protein'.
authors: School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK.
authors: Veronika
authors: V
authors: Majcher
authors: School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK.
authors: Alice
authors: A
authors: Goode
authors: School of Veterinary Medicine and Science, Sutton Bonington Campus, University of Nottingham, LE12 5RD, UK.
authors: Victoria
authors: V
authors: James
authors: School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK. Electronic address: robert.layfield@nottingham.ac.uk.
authors: Robert
authors: R
authors: Layfield
mesh_terms: D000690:Amyotrophic Lateral Sclerosis / Q000503:physiopathology*; D000818:Animals; D001343:Autophagy / Q000502:physiology*; D057174:Frontotemporal Lobar Degeneration / Q000503:physiopathology*; D006801:Humans; D009419:Nerve Tissue Proteins / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*
chemical_list: D009419:Nerve Tissue Proteins
keywords: ALS; Autophagy; FTLD; Optineurin; SQSTM1/p62; Stress granules; Ubiquilin; VCP