Self-oligomerization regulates stability of survival motor neuron protein isoforms by sequestering an SCFSlmb degron-Reference-Cited by-同舟云学术

Self-oligomerization regulates stability of survival motor neuron protein isoforms by sequestering an SCFSlmb degron

Published:2018-01-15 Issue:2 Volume:29 Page:96-110
ISSN:1059-1524
Container-title:Molecular Biology of the Cell
language:en
Short-container-title:MBoC

Author:

Gray Kelsey M.¹²,Kaifer Kevin A.³,Baillat David⁴,Wen Ying²,Bonacci Thomas R.¹⁵,Ebert Allison D.⁶,Raimer Amanda C.¹²,Spring Ashlyn M.²,Have Sara ten⁷,Glascock Jacqueline J.³,Gupta Kushol⁸,Van Duyne Gregory D.⁸,Emanuele Michael J.¹⁵,Lamond Angus I.⁷,Wagner Eric J.⁴,Lorson Christian L.³,Matera A. Gregory¹²

Affiliation:

1. Curriculum in Genetics and Molecular Biology and Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599

2. Integrative Program in Biological and Genome Sciences, Department of Biology and Department of Genetics, University of North Carolina, Chapel Hill, NC 27599

3. Molecular Pathogenesis and Therapeutics Program, Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Missouri, Columbia, MO 65211

4. Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77550

5. Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599

6. Department of Cell Biology, Neurobiology and Anatomy, Medical College of Wisconsin, Milwaukee, WI 53226

7. Centre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee DD15EH, UK

8. Department of Biochemistry and Biophysics, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104

Abstract

SMN protein levels inversely correlate with the severity of spinal muscular atrophy. The SCFSlmbE3 ligase complex interacts with a degron embedded within the C-terminal self-oligomerization domain of SMN. The findings elucidate a model whereby accessibility of the SMN degron is regulated by self-multimerization.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

Reference119 articles.

1. Plastin 3 ameliorates spinal muscular atrophy via delayed axon pruning and improves neuromuscular junction functionality

2. Molecular Mechanisms of Neurodegeneration in Spinal Muscular Atrophy

3. An optimized transgenesis system for Drosophila using germ-line-specific C31 integrases

4. SMN, profilin IIa and plastin 3: A link between the deregulation of actin dynamics and SMA pathogenesis

5. A critical smn threshold in mice dictates onset of an intermediate spinal muscular atrophy phenotype associated with a distinct neuromuscular junction pathology

Cited by 28 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Ubiquitination Insight from Spinal Muscular Atrophy—From Pathogenesis to Therapy: A Muscle Perspective;International Journal of Molecular Sciences;2024-08-13

2. U1 snRNA interactions with deep intronic sequences regulate splicing of multiple exons of spinal muscular atrophy genes;Frontiers in Neuroscience;2024-07-12

3. Polymerization of ZBTB transcription factors regulates chromatin occupancy;Molecular Cell;2024-07

4. Chaperoning the chaperones: Proteomic analysis of the SMN complex reveals conserved and etiologic connections to the proteostasis network;2024-05-16

5. Dysregulation of innate immune signaling in animal models of spinal muscular atrophy;BMC Biology;2024-04-25