| Gene information | Literature | Expression | lncRNA | Mutation | Homolog |
Basic Information | |
|---|---|
Gene ID | 7175 |
Name | TPR |
Synonymous | translocated promoter region, nuclear basket protein;TPR;translocated promoter region, nuclear basket protein |
Definition | NPC-associated intranuclear protein|megator|nuclear pore complex-associated protein TPR|nucleoprotein TPR|translocated promoter region (to activated MET oncogene)|translocated promoter region protein|tumor potentiating region |
Position | 1q25 |
Gene type | protein-coding |
Title | Abstract |
| TRK-T1 is a novel oncogene formed by the fusion of TPR and TRK genes in human papillary thyroid carcinomas. | We have recently reported the frequent activation of the TRK oncogene in human papillary thyroid carcinoma. In this paper we describe the isolation and characterization of one of the thyroid TRK oncogenes, designated TRK-T1. A 1746-bp-long cDNA was isolated from a library derived from a primary transformant. The cDNA was able to induce foci in NIH3T3 cells. Sequence analysis revealed that TRK-T1 is created by an intrachromosomal rearrangement that juxtaposes the 5 end of the TPR gene to the TRK tyrosine kinase domain. The resulting hybrid mRNA contains 598 nucleotides of the TPR gene and 1148 nucleotides of the TRK proto-oncogene. TRK-T1 mRNA encodes a protein of 55 kDa reacting with antibodies against the carboxy terminus of the proto-TRK protein. We show also the involvement of TPR in the generation of another TRK-T oncogene. |
| Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex. | From a panel of monoclonal antibodies raised against fractions of rat liver nuclear envelopes (NEs), we have identified an antibody, RL30, which reacts with novel nuclear pore complex (NPC) antigens that are not O-glycosylated. By immunofluorescence staining of cultured cells, RL30 reacts exclusively with the NE in a punctate pattern that largely coincides with that of identified NPC proteins. RL30 labels only the cytoplasmic surface of the NPC in immunogold electron microscopy, predominantly in peripheral regions nearby the cytoplasmic ring. In immunoblots of isolated rat liver NEs and cultured rat cells, RL30 recognizes a 265-kD band, as well as a series of 175-265-kD bands in rat liver NEs that are likely to be proteolytic products of p265. Sequencing of peptides from the 175- and 265-kD RL30 antigens of rat liver revealed that they are both closely related to human Tpr, a protein whose amino-terminal 150-250 amino acids appear in oncogenic fusions with the kinase domains of the met, trk, and raf protooncogenes. We found that in vitro translation of human Tpr mRNA yields a major 265-kD band. Considered together, these data indicate that the 265-kD RL30 antigen in the NPC is the rat homologue of Tpr. Interestingly, Tpr contains an exceptionally long predicted coiled coil domain (approximately 1600 amino acids). The localization and predicted structure of Tpr suggest that it is a component of the cytoplasmic fibrils of the NPC implicated in nuclear protein import. Immunofluorescence microscopy shows that during NPC reassembly at the end of mitosis, Tpr becomes concentrated at the NE significantly later than O-linked glycoproteins, including p62. This indicates that reassembly of the NPC after mitosis is a stepwise process, and that the Tpr-containing peripheral structures are assembled later than p62. |