The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia.
Multiple sequence alignment has revealed the presence of a sequence domain of approximately 80 amino acids in two molecules, spartin and spastin, mutated in hereditary spastic paraplegia. The domain, which corresponds to a slightly extended version of the recently described ESP domain of unknown function, was also identified in VPS4, SKD1, RPK118, and SNX15, all of which have a well established and consistent role in endosomal trafficking. Recent functional information indicates that spastin is likely to be involved in microtubule interaction. With this new information relating to its likely function, we propose the more descriptive name 'MIT' (contained within microtubule-interacting and trafficking molecules) for the domain and predict endosomal trafficking as the principal functionality of all molecules in which it is present.
Ciccarelli
Francesca D
FD
European Molecular Biology Laboratory, Meyerhofstr. 1, 69012 Heidelberg, Germany.
Proukakis
Christos
C
Patel
Heema
H
Cross
Harold
H
Azam
Shakil
S
Patton
Michael A
MA
Bork
Peer
P
Crosby
Andrew H
AH
D000251:Adenosine Triphosphatases; D000595:Amino Acid Sequence; D002135:Calcium-Binding Proteins / Q000235:genetics*; D018797:Cell Cycle Proteins; D011992:Endosomes / Q000378:metabolism; D019143:Evolution, Molecular; D006801:Humans; D017434:Protein Structure, Tertiary / Q000235:genetics*; D011506:Proteins / Q000235:genetics*; D016415:Sequence Alignment; D015419:Spastic Paraplegia, Hereditary / Q000235:genetics*; D000074181:Spastin
D002135:Calcium-Binding Proteins; D018797:Cell Cycle Proteins; D011506:Proteins; C464787:SPART protein, human; D000251:Adenosine Triphosphatases; D000074181:Spastin; C400283:SPAST protein, human