許多神經學疾病與粒線體運輸在軸突上的改變有關。因此了解粒線體動力學是如何在分子層次上被調節相當重要。自候選基因篩選中，我們找出了能夠調節粒線體形態及動力學的蛋白SFXN-1.2。有趣的是，SFXN-1.2是與阿茲海默症、帕金森氏症相關的人類蛋白Sideroflexin 1/3的直系同源基因。我們的研究結果顯示SFXN-1.2會透過一個與夏柯-馬利-杜斯氏症有關的蛋白CX32(連接蛋白32)和驅動蛋白-3 KIF1A(UNC-104)結合。儘管SFXN-1.2與CX32影響了粒線體動力學，他們也能單獨影響分子馬達UNC-104的運動。雖然已知UNC-104透過其PH結構域與突觸囊泡結合，我們發現這個結構域並未在連結分子馬達與粒線體中扮演任何角色。更重要的是SFXN-1.2對突觸囊泡的運輸沒有任何影響，這強調了其角色對於粒線體運輸的專一性。透過酵母菌雙雜交系統、共免疫沉澱與雙螢光分子互補試驗，我們精確化了UNC-104/CX32/SFXN-1.2複合體的關鍵互動架構。在我們的模型中驅動蛋白-1與驅動蛋白-3相互合作地運送粒線體，因為miro-1和trak-1的基因敲落進一步加強了unc-104突變對粒線體運動的負面效應。SFXN-1.2的突變明顯地導致秀麗隱桿線蟲的運動與感覺神經缺陷，影響了該動物的碰觸反應及限制其身體動作。最後我們揭露粒線體生物能量學與粒線體自噬均未受到sfxn-1.2突變的影響

粒線體與中間絲(IF)的聚集經常發生在不平衡的軸突運輸中，並導致許多型態的神經學疾病。目前對於神經性中間絲與粒線體運動是否存在關聯仍然了解甚少。在秀麗隱桿線蟲的11個細胞質中間絲家族蛋白中，IFB-1特別令人感興趣，因為其在部分的感覺神經中表現。IFB-1的減少導致了輕微的染劑填充缺陷、顯著的化學趨向性缺陷以及壽命的減少。感覺神經發育也受到了影響，而粒線體運輸亦減慢並造成這些胞器密度的減少。IFB-1突變株的粒線體傾向於神經中簇聚成群有可能與粒線體分裂、融合機制無關。帶有ifb-1突變基因的線蟲被檢測出其粒線體膜電位的下降。膜電位似乎也在運輸中扮演了重要的角色，因為給予氰化羰對三氟甲氧苯基腙的處理增加了粒線體在方向上的變換。總結來說，我們提出了一個模型，其中神經性中間絲可能為了穩定與平衡的運輸，在粒線體於神經的長距離運輸中作為其重要的(瞬間的)錨點。

Various neurological diseases are linked to changes in mitochondrial trafficking in axons. Thus, it is crucial to understand how the dynamics of mitochondria are regulated on the molecular level. From a candidate screen, we identified protein SFXN-1.2 to regulate both morphologies as well as dynamics of mitochondria. Interestingly, SFXN-1.2 is an ortholog of human Sideroflexin 1/3 associated with Alzheimer's disease and Parkinson's disease. We show that SFXN-1.2 binds to kinesin-3 KIF1A(UNC-104) via CX32 (Connexin 32), a protein known to be linked to Charcot-Marie-Tooth diseases. While SFXN-1.2 and CX32 affect the dynamics of mitochondria, they also affect the motility of the molecular motor UNC-104 alone. Though it is known that UNC-104 binds to synaptic vesicles via its PH domain, we found no role of this domain in linking the motor to mitochondria. Critically, SFXN-1.2 has no effect on synaptic vesicle trafficking under-lining the specificity of its role on mitochondria transport. From yeast two-hybrid, co-immunoprecipitation, and bimolecular fluorescent complementation assays, we narrowed down critical interaction schemes of the UNC-104/CX32/SFXN-1.2 complex. In our model, kinesin-1 and kinesin-3 act cooperatively to transport mitochondria since the knocking down of miro-1 and trak-1 further enhances the negative effect of unc-104 mutations on mitochondrial motility. Strikingly, mutations in SFXN-1.2 lead to motor- and sensory neuron defects in C. elegans affecting the animal’s touch responses as well as restricting body movements. Lastly, we revealed that neither mitochondrial bioenergetics nor mitophagy are affected by the sfxn-1.2 mutation.

Mitochondria and intermediate filament (IF) accumulations often occur during imbalanced axon-al transport leading to various types of neurological diseases. It is still poorly understood whether a link between neuronal IFs and mitochondrial mobility exist. In Caenorhabditis elegans, among the 11 cytoplasmic IF family proteins, IFB-1 is of particular interest as it is expressed in a subset of sensory neurons. Depletion of IFB-1 leads to mild dye-filling and significant chemotaxis de-fects as well as reduced life span. Sensory neuron development is affected and mitochondrial transport is slowed down leading to reduced densities of these organelles. Mitochondria tend to cluster in neurons of IFB-1 mutants likely independent of the fission and fusion machinery. Mitochondrial membrane potential is measurably reduced in worms carrying mutations in the ifb-1 gene. Membrane potential also seems to play a role in transport such as carbonyl cyanide p-(trifluoromethoxy)phenylhydrazone treatment led to increased directional switching of mitochondria. In summary, we propose a model in which neuronal IFs may serve as critical (transient) anchor points for mitochondria during their long-range transport in neurons for steady and balanced transport.

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