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Intraflagellar transport protein 52 homolog (IFT52) is a conserved, proline-rich protein central to the function and structural integrity of the IFT-B core complex, which is essential for ciliogenesis (the formation of cilia) and intraflagellar transport, a bi-directional mechanism that assembles and maintains cilia and flagella in eukaryotic cells[1][2][4]. IFT52 acts as a scaffold protein within the IFT-B complex, mediating interactions between several core subunits (including IFT81/74/27/25 and IFT88/70/52/46) and recruiting structural components and molecular motors necessary for ciliary assembly and maintenance[1][2][5]. It is required for the biosynthesis and function of cilia, critical for cellular motility, sensory signaling, and developmental signal transduction pathways. Mutations in IFT52 cause ciliopathies, including skeletal disorders characterized by abnormal ciliary function[3][4]. Currently, IFT52 is not a direct therapeutic target and has no known small-molecule or biologic modulators. Key structural features include an N-terminal GIFT domain, a central disordered region (responsible for many protein-protein interactions), and a C-terminal domain that forms a heterodimer with IFT46[1][2]. IFT52 is conserved from unicellular organisms like Chlamydomonas to vertebrates, emphasizing its essential role in ciliary biology[3].
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