Cytoplasmic linker protein 1 (CLIP-170) (CLIP-170)

Cytoplasmic linker protein 1 (CLIP-170) is a prominent member of the microtubule-plus-end-tracking protein (+TIP) family, essential for the regulation of microtubule dynamics and cellular organization [1]. It functions by specifically binding to the growing plus ends of microtubules, where it promotes polymerization and facilitates the linkage of microtubules to various cellular structures, including the actin cytoskeleton and endocytic vesicles [3]. In clinical oncology, CLIP-170 is a significant therapeutic target primarily through its involvement in oncogenic fusions, most notably the CLIP1-ALK fusion identified in non-small cell lung cancer (NSCLC) [2]. This fusion results in the constitutive activation of the ALK tyrosine kinase, driving tumor progression and making it sensitive to ALK inhibitors such as crizotinib and alectinib [2]. Beyond its role in cancer, CLIP-170 is critical for neuronal migration and axonal transport, with its dysregulation linked to neurodegenerative diseases like Amyotrophic Lateral Sclerosis (ALS) and various brain malformations [4]. Consequently, while it is not a traditional cell-surface receptor, its role as a scaffold and regulator makes it a vital component in both developmental biology and precision medicine [1, 4].

Other names

CLIP1RestinRSNCLIP-170

Inhibition of the ALK kinase domain within the CLIP1-ALK fusion protein.