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Fam134c and Fam134b shape axonal endoplasmic reticulum architecture in vivo. | LitMetric

AI Article Synopsis

  • Endoplasmic reticulum (ER) remodeling is crucial for cell organization, and a process called ER-phagy selectively removes damaged ER to maintain its structure and function.
  • The FAM134 protein family (FAM134A, FAM134B, FAM134C) is involved in this process, with mutations in FAM134B linked to a specific neuropathy in humans, while the functions of the other proteins are less understood.
  • Research using mouse models reveals that deleting both FAM134B and FAM134C results in severe neuromuscular and sensory degeneration, emphasizing their critical role in maintaining the tubular structure of ER in motor and sensory neuron axons.

Article Abstract

Endoplasmic reticulum (ER) remodeling is vital for cellular organization. ER-phagy, a selective autophagy targeting ER, plays an important role in maintaining ER morphology and function. The FAM134 protein family, including FAM134A, FAM134B, and FAM134C, mediates ER-phagy. While FAM134B mutations are linked to hereditary sensory and autonomic neuropathy in humans, the physiological role of the other FAM134 proteins remains unknown. To address this, we investigate the roles of FAM134 proteins using single and combined knockouts (KOs) in mice. Single KOs in young mice show no major phenotypes; however, combined Fam134b and Fam134c deletion (Fam134b/c), but not the combination including Fam134a deletion, leads to rapid neuromuscular and somatosensory degeneration, resulting in premature death. Fam134b/c mice show rapid loss of motor and sensory axons in the peripheral nervous system. Long axons from Fam134b/c mice exhibit expanded tubular ER with a transverse ladder-like appearance, whereas no obvious abnormalities are present in cortical ER. Our study unveils the critical roles of FAM134C and FAM134B in the formation of tubular ER network in axons of both motor and sensory neurons.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11316074PMC
http://dx.doi.org/10.1038/s44319-024-00213-7DOI Listing

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