D
IPR009686

Senescence/spartin-associated, C-terminal

InterPro entry
Short nameSenescence/spartin_C

Description

This is the AAA ATPase domain found at the C-terminal of plant senescence-associated proteins and spartin. In Hemerocallis, petals have a genetically based program that leads to senescence and cell death approximately 24 hours, after the flower opens, and it is believed that senescence proteins produced around that time have a role in this program
[1]
. This domain is also found at the C-terminal of Spartin, a protein from higher vertebrates associated with endosomal trafficking and microtubule dynamics
[2]
. Spartin functions presynaptically with endocytic adaptor Eps15 to regulate synaptic growth and function. Mutations in human spartin gene cause Troyer syndrome, a hereditary spastic paraplegia
[3]
. This AAA ATPase domain similar to other AAA proteins contain an α/β nucleotide-binding domain (NBD) and a smaller four-helix bundle domain (HBD)
[4]
. Uniquely among AAA structures, spastin has two helices (N-terminal α1 and C-terminal α11) that embrace the NBD
[4]
.

References

1.Identification of senescence-associated genes from daylily petals. Panavas T, Pikula A, Reid PD, Rubinstein B, Walker EL. Plant Mol. Biol. 40, 237-48, (1999). View articlePMID: 10412903

2.The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia. Ciccarelli FD, Proukakis C, Patel H, Cross H, Azam S, Patton MA, Bork P, Crosby AH. Genomics 81, 437-41, (2003). View articlePMID: 12676568

3.Spartin regulates synaptic growth and neuronal survival by inhibiting BMP-mediated microtubule stabilization. Nahm M, Lee MJ, Parkinson W, Lee M, Kim H, Kim YJ, Kim S, Cho YS, Min BM, Bae YC, Broadie K, Lee S. Neuron 77, 680-95, (2013). PMID: 23439121

4.Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin. Roll-Mecak A, Vale RD. Nature 451, 363-7, (2008). View articlePMID: 18202664

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