Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein
Cysteine-string protein (CSP) is an extensively palmitoylated DnaJ-family chaperone, which
exerts an important neuroprotective function. Palmitoylation is required for the intracellular
sorting and function of CSP, and thus it is important to understand how this essential
modification of CSP is regulated. Recent work identified 23 putative palmitoyl transferases
containing a conserved DHHC domain in mammalian cells, and here we show that
palmitoylation of CSP is enhanced specifically by co-expression of the Golgi-localized …
exerts an important neuroprotective function. Palmitoylation is required for the intracellular
sorting and function of CSP, and thus it is important to understand how this essential
modification of CSP is regulated. Recent work identified 23 putative palmitoyl transferases
containing a conserved DHHC domain in mammalian cells, and here we show that
palmitoylation of CSP is enhanced specifically by co-expression of the Golgi-localized …
以上显示的是最相近的搜索结果。 查看全部搜索结果