gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Zinc finger, FYVE domain containing 27

Protrudin, SPG33, ZFYVE27
This gene encodes a protein with several transmembrane domains, a Rab11-binding domain and a lipid-binding FYVE finger domain. The encoded protein appears to promote neurite formation. A mutation in this gene has been reported to be associated with hereditary spastic paraplegia, however the pathogenicity of the mutation, which may simply represent a polymorphism, is unclear. [provided by RefSeq, Mar 2010] (from NCBI)
Sponsored links
Top mentioned proteins: KIF5B, spastin, SPG31, SPG3A, Rab11
Papers on Protrudin
Protrudin regulates endoplasmic reticulum morphology and function associated with the pathogenesis of hereditary spastic paraplegia.
Nakayama et al., Fukuoka, Japan. In J Biol Chem, 2014
The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia (SPG) 33.
Molecular epidemiology and clinical spectrum of hereditary spastic paraplegia in the Japanese population based on comprehensive mutational analyses.
Tsuji et al., Tokyo, Japan. In J Hum Genet, 2014
To elucidate molecular epidemiology of HSP in the Japanese population, we have conducted mutational analyses of 16 causative genes of HSP (L1CAM, PLP1, ATL1, SPAST, CYP7B1, NIPA1, SPG7, KIAA0196, KIF5A, HSPD1, BSCL2, SPG11, SPG20, SPG21, REEP1 and ZFYVE27) using resequencing microarrays, array-based comparative genomic hybridization and Sanger sequencing.
Identification and characterization of a neuron-specific isoform of protrudin.
Nakayama et al., Fukuoka, Japan. In Genes Cells, 2014
Protrudin is a membrane protein that regulates polarized vesicular transport.
Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation.
Blackstone et al., Bethesda, United States. In Proc Natl Acad Sci U S A, 2013
Here, we show that the SPG33 protein protrudin contains hydrophobic, intramembrane hairpin domains, interacts with tubular ER proteins, and functions in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections.
Phosphoinositides differentially regulate protrudin localization through the FYVE domain.
Heo et al., Taejŏn, South Korea. In J Biol Chem, 2012
Protrudin is a FYVE (Fab 1, YOTB, Vac 1, and EEA1) domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia.
Hereditary spastic paraplegias with autosomal dominant, recessive, X-linked, or maternal trait of inheritance.
Review
Stevanin et al., Vienna, Austria. In J Neurol Sci, 2012
Among the AD-SPGs, 40-45% of patients carry mutations in the SPAST-gene (SPG4) and 10% in the ATL1-gene (SPG3), while the other 9 genes are more rarely involved (NIPA1 (SPG6), KIAA0196 (SPG8), KIF5A (SPG10), RNT2 (SPG12), SPGD1 (SPG13), BSCL2 (SPG17), REEP1 (SPG31), ZFYVE27 (SPG33, debated), and SLC33A1 (SPG42, debated)).
Role of spastin and protrudin in neurite outgrowth.
GeneRIF
Ma et al., Beijing, China. In J Cell Biochem, 2012
findings indicate that protrudin interacts with spastin and induces axon formation through its N-terminal domain. Moreover, protrudin and spastin may work together to play an indispensable role in motor axon outg
Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation.
GeneRIF
Nakayama et al., Fukuoka, Japan. In Mol Biol Cell, 2011
Protrudin and KIF5 interact in mouse brain.Protrudin-KIF5 complex contributes to the vesicular transport in neurons.
Oligomerization of ZFYVE27 (Protrudin) is necessary to promote neurite extension.
Mannan et al., Göttingen, Germany. In Plos One, 2010
ZFYVE27 (Protrudin) was originally identified as an interacting partner of spastin, which is most frequently mutated in hereditary spastic paraplegia.
Promotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated protein.
GeneRIF
Nakayama et al., Fukuoka, Japan. In J Biol Chem, 2009
VAP-A is an important regulator both of the subcellular localization of protrudin and of its ability to stimulate neurite outgrowth.
The role of ZFYVE27/protrudin in hereditary spastic paraplegia.
GeneRIF
Rugarli et al., In Am J Hum Genet, 2008
The role of ZFYVE27/protrudin in hereditary spastic paraplegia is reported.
Regulation of apoptosis and neurite extension by FKBP38 is required for neural tube formation in the mouse.
Nakayama et al., Fukuoka, Japan. In Genes Cells, 2008
To explore the mechanisms underlying these characteristics, we screened for proteins that interact with FKBP38 in the yeast two-hybrid system and thereby identified protrudin, a protein that promotes process formation by regulating membrane trafficking.
Refinement of the SPG9 locus on chromosome 10q23.3-24.2 and exclusion of candidate genes.
Seri et al., Bologna, Italy. In Eur J Neurol, 2008
In the same region, two other forms of HSP have been recently mapped: SPG27 and SPG33.
Lack of spartin protein in Troyer syndrome: a loss-of-function disease mechanism?
Blackstone et al., Bethesda, United States. In Arch Neurol, 2008
BACKGROUND: Hereditary spastic paraplegias (SPG1-SPG33) are characterized by progressive spastic weakness of the lower limbs.
A novel candidate locus on chromosome 11p14.1-p11.2 for autosomal dominant hereditary spastic paraplegia.
Tang et al., Changsha, China. In Chin Med J (engl), 2008
RESULTS: The known autosomal dominant loci of SPG3A, SPG4, SPG6, SPG8, SPG9, SPG10, SPG12, SPG13, SPG17, SPG19, SPG29, SPG31 and SPG33 were excluded by linkage analysis.
Protrudin induces neurite formation by directional membrane trafficking.
Impact
GeneRIF
Nakayama et al., Fukuoka, Japan. In Science, 2006
protrudin regulates Rab11-dependent membrane recycling to promote the directional membrane trafficking required for neurite formation [protrudin]
ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia.
GeneRIF
Engel et al., Göttingen, Germany. In Am J Hum Genet, 2006
Mutation affects neuronal intracellular trafficking in the corticospinal tract, which is consistent with the pathology of hereditary spastic paraplegia.
share on facebooktweetadd +1mail to friends