Nucleoporin NDC1 (NDC1)

Nucleoporin NDC1 (NDC1) is an evolutionarily conserved, integral membrane nucleoporin and a core structural component of the nuclear pore complex (NPC), where it regulates the assembly, insertion, and stability of the NPC in the nuclear envelope[1][5]. NDC1 anchors the soluble nucleoporin ALADIN and functions as a critical bridge, facilitating selective protein import into the nucleus and maintaining nuclear-cytoplasmic compartmentalization[1][3]. Its topology features six transmembrane segments and multiple cytoplasm- and nucleoplasm-exposed domains, consistent with its role as a scaffold for complex assembly and membrane integration[2]. Loss or mutation of NDC1 disrupts normal NPC function, causes mislocalization of NPC constituents, and is linked to disorders such as triple A syndrome-like diseases and neuropathy[1][2][3]. In cancer, notably hepatocellular carcinoma, aberrant NDC1 overexpression can potentiate oncogenic pathways promoting cell proliferation and invasion[1]. NDC1 is also crucial in male gametogenesis through interactions with septin proteins that are vital for correct nuclear membrane morphology during sperm development[1]. No approved therapies or drugs target NDC1 directly, and it is not classified as a typical small molecule drug target (such as a receptor or enzyme)[1][5]. Summary: Nucleoporin NDC1 (NDC1, also known as TMEM48) is an evolutionarily conserved, integral transmembrane nucleoporin that is vital for nuclear pore complex assembly, nuclear envelope integrity, and nucleocytoplasmic transport; although highly relevant to disease and cellular biology, it is not currently considered a direct therapeutic target nor a receptor/enzyme[1][2][5].

Other names

TMEM48Transmembrane protein 48hNDC1FLJ10407NET3Nuclear division cycle 1 homolog (S. cerevisiae)nuclear division cycle 1 homolog