小分子鳥糞嘌呤核苷酸結合蛋白質 (small GTPase) 腺嘌呤核苷二磷酸核
糖化因子 (ADP-ribosylation factors; Arfs)是一個約 20-kDa 的蛋白質，Arf 主要負責調控並參與胞內囊泡運輸的路徑，Arf 如同 Small GTPase 能夠被他們的調控蛋白質鳥糞嘌呤核苷酸交換因子 (guanine nucleotide-exchange factors, GEF)上的 Sec7 功能域催活，使得失活態的 Arf (結合 GDP)轉換為活化態的 Arf (轉為結合 GTP)。鳥糞嘌呤核苷酸交換因子 BIG1 和 BIG2 (brefeldin A-inhibited
guanine nucleotide-exchange factors, BIG)，最初是在小牛腦組織內約 670 kDa 的蛋白質複合物中被發現的，在 BIG1 和 BIG2 主要負責催活 Arf 的 Sec7 功能域上有著高達 90%的 identity，除了 Sec7 功能域外，其他幾個在 N 端及 C 端的保守功能域的功能都鮮為人知。因此，我們透過酵母菌雙雜交系統，並利用BIG1NSec7 (a.a. 1-885,包含 Sec7 domain) and BIG1C (a.a. 886-1849)當作誘餌蛋白質與人類胚胎大腦 cDNA 庫進行交互作用的篩選。本實驗發現了多個候選蛋白質，包括了微管相聯蛋白質 1B ( microtubule-associated protein 1B, MAP1B)的輕鏈(light chain 1, LC1)與 α-tubulin 等和微管組成相關的蛋白質；進一步利用酵母菌雜交研究出 MAP1B-LC1、α-tubulin 與 BIG1 交互作用的胺基酸序列，MAP1B-LC1與BIG1的Sec7功能域有專一性的交互作用，而α-tubulin與BIG1N端片段有交互作用，與 Sec7 域則無。微管結構的組成中，α-tubulin 便是其主要的聚合物之一，而 MAP1B 也多次被研究發現與微管的發展、穩定相關，並在神經細胞的軸突發育延伸、神經細胞遷移扮演重要角色。我們希望能透過這些新的交互作用的發現，在未來能更加明白 BIG1 如何調控廣範圍、長距離的胞內運輸等生理機制。

ADP-ribosylation factors (Arfs) are a family of 20-kDa guanine nucleotide-binding proteins which are involved in regulation of several pathways of intracellular trafficking.
Similar with other small GTPase, activation of Arfs is catalyzed by the Sec7 domain of Arf guanine nucleotide exchange factors (GEFs), which can catalyze the replacement of Arf-bound GDP by GTP. Two brefeldin A (BFA)-inhibited guanine nucleotide-exchange proteins, BIG1 (~200-kDa) and BIG2 (~190-kDa), were purified together in >670-kDa
multiprotein complexes from bovine brain cytosol. BIG1 and BIG2 were 90% identical in the ~200-amino-acid Sec7 domains. Besides the catalytic GEF activity of the Sec7 domain,
there are additional highly conserved sequences in the N and C termini of BIG1 and BIG2 that remain less defined. Here, I used the yeast two-hybrid system which BIG1NSec7 (a.a.
1-885, contained Sec7 domain) and BIG1C (a.a. 886-1849) as bait to screen interaction with a human fetal brain cDNA library respectively. We identified several candidate
proteins which related to microtubule assembly, including microtubule-associated protein 1B-light chain 1 (MAP1B-LC1, a.a. 2262-2468) and α-tubulin. Interactive regions of BIG1
to MAP1B-LC1 and α-tubulin were narrowed down by yeast two-hybrid assay. Sec7 domain (a.a. 698-885) of BIG1 is responsible for interaction with MAP1B-LC1, and α-tubulin interacted with the N-terminal structures, but not Sec7 domain of BIG1. Alpha-tubulin is well known as a major component of microtubules. Function of MAP1B are reported to regulate the polymerization of microtubule and actin microfilaments, and involves in axonal elongation, neuronal migration, and axonal guidance. These newly recognized interactions should let us understand better the mechanisms through which BIG1 may integrate local events in membrane trafficking with longer-range transport processes.

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