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SUMMARY:Solving the 50-years-old puzzle of the mechanism of tubulin detyro
 sination
DTSTART:20241001T161500
DTEND:20241001T171500
DTSTAMP:20260926T093042Z
UID:5ce6b3054373abde89ede3ec9d9c2fca7efc8ef30f9dfdd8c4893fd0
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. A. Tassos Perrakis - Utrecht University\nMicrotubules ar
 e a major component of the cytoskeleton and can accumulate a plethora of m
 odifications. The microtubule detyrosination cycle is one of these modific
 ations\; it involves the enzymatic removal of the C-terminal tyrosine of 
 α-tubulin on assembled microtubules and the re-ligation of tyrosine on de
 tyrosinated tubulin dimers. This modification cycle has been implicated in
  cardiac disease\, neuronal development\, and mitotic defects. The enzymes
  responsible for microtubule detyrosination remains a long-sought mystery 
 for well-over four decades since the biochemical process of detyrosination
  was described. The vasohibins and their co-factor Small Vasohibin Binding
  Protein (SVBP)\, are cysteine peptidases which were originally known as e
 xtracellular angiogenesis regulators\, and were the first tubulin detyrosi
 nases we discovered. Later\, the Microtubule-Associated Tyrosine CArboxyPe
 ptidase (MATCAP) and a close homologue (TMCP2) were identified as zinc met
 alloproteases that can cleave α (and β)tubulin tails. The structures of 
 the catalytic domains of members of the two evolutionary unrelated enzyme 
 families were determined by X-ray crystallography\, establishing the corre
 sponding cleavage mechanisms. Both families act preferentially on microtub
 ules rather than on tubulin dimers\, and the cryo-electron microscopy stru
 ctures of vasohibins and MATCAP bound to microtubules\, were key to unders
 tand fundamental differences: the vasohibins catalytic domain interacts bo
 th with the α-tubulin monomer whose tail will be cleaved and with α-tubu
 lin of the adjacent protofilament\, but MATCAP binds to adjacent tubulin d
 imers along a single protofilament. The current information is key to furt
 her study how these enzymes interplay with other modifications and define 
 the tubulin code.
LOCATION:CH G1 495 https://plan.epfl.ch/?room==CH%20G1%20495
STATUS:CONFIRMED
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