Passafaro M, Sala C, Niethammer M, Sheng M
Howard Hughes Medical Institute and Department of Neurobiology, Massachusetts General Hospital and Harvard Medical School, HHMI/Wellman 423, 50 Blossom Street, Boston, Massachusetts 02114, USA.
Nat Neurosci. 1999 Dec;2(12):1063-9. doi: 10.1038/15990.
CRIPT is a postsynaptic protein that binds selectively to the third PDZ domain (PDZ3) of PSD-95. Here we show that CRIPT also binds directly to microtubules, thereby linking PSD-95 to the microtubule cytoskeleton. Disrupting the CRIPT-PSD-95 interaction in cultured hippocampal neurons with a PDZ3-specific peptide prevented the association of PSD-95 with microtubules and inhibited the synaptic clustering of PSD-95, chapsyn-110/PSD-93 and GKAP (a PSD-95-binding protein). However, the number of synapses and the synaptic clustering of NMDA receptors were unaffected, suggesting that PSD-95-family proteins are not essential for the maintenance of synapses and the synaptic localization of NMDA receptors.
CRIPT是一种突触后蛋白，它选择性地与PSD-95的第三个PDZ结构域（PDZ3）结合。在此我们表明，CRIPT还直接与微管结合，从而将PSD-95与微管细胞骨架相连。用PDZ3特异性肽破坏培养的海马神经元中CRIPT与PSD-95的相互作用，可阻止PSD-95与微管的结合，并抑制PSD-95、chapsyn-110/PSD-93和GKAP（一种与PSD-95结合的蛋白）的突触聚集。然而，突触数量和NMDA受体的突触聚集不受影响，这表明PSD-95家族蛋白对于突触的维持和NMDA受体的突触定位并非必不可少。
