Target Name: CDC37L1
NCBI ID: G55664
Other Name(s): cell division cycle 37 like 1, HSP90 cochaperone | cell division cycle 37 homolog-like 1 | HARC | Cell division cycle 37 like 1, HSP90 cochaperone | Hsp90-associating relative of Cdc37 | Hsp90 co-chaperone Cdc37-like 1 | CDC37 cell division cycle 37 homolog-like 1 | CD37L_HUMAN | cell division cycle 37 like 1 | FLJ20639 | CDC37B | RP11-6J24.5

CD37L1: A Promising Drug Target and Biomarker for Cell Division Cycle 37 Like 1

Cell division cycle (CDC) is a critical process that regulates cell growth, proliferation, and differentiation. The CDC is composed of three phases: G1, S, and G2. Cell division cycle 37 like 1 (CDC37L1) is a protein that plays a significant role in the G1 phase of the CDC. It is a cochaperone that helps to transport and regulate the movement of chromosomes during the S phase. CD37L1 is also known as HSP90 cochaperone, which is a protein that contains a unique nucleotide-binding oligomerization domain (NBO domain) and a hydrophobic transmembrane region (TMD).

The HSP90 protein is a heat-activated protein that can exist in two interconvertible forms: a monomeric form and a dimeric form. The monomeric form is predominantly localized to the cytoplasm, while the dimeric form is primarily localized to the nucleus. CD37L1 is a 14-kDa protein that is predominantly localized to the nucleus, and it interacts with the HSP90 dimeric form.

CD37L1 functions as a cochaperone for the HSP90 dimeric form during the S phase of the CDC. It helps to regulate the movement of chromatin during the S phase by interacting with the NBO domain of HSP90. The NBO domain is a unique protein domain that contains a specific sequence of amino acids that is known to play a critical role in the association of nucleotides with the protein. The NBO domain is responsible for the protein's stability, localization, and interaction with other proteins.

CD37L1 has been identified as a potential drug target due to its unique functions in the CDC. One of the main reasons for its potential as a drug target is its involvement in the regulation of cell proliferation. CD37L1 has been shown to play a role in the regulation of cell cycle progression by interacting with the growth factors, such as Wnt, TGF-β, and NF-kappa-B.

Another reason for its potential as a drug target is its involvement in the regulation of cell survival. CD37L1 has been shown to play a role in the regulation of cell survival by interacting with the anti-apoptotic protein, Bcl-2.

CD37L1 has also been shown to play a role in the regulation of cell adhesion. CD37L1 has been shown to interact with the adhesion molecule, E-cadherin.

CD37L1 is a 14-kDa protein that is predominantly localized to the nucleus during the S phase of the CDC. It functions as a cochaperone for the HSP90 dimeric form during the S phase. CD37L1 has been shown to play a role in the regulation of cell cycle progression, cell survival, and cell adhesion. As a result, CD37L1 is a promising drug target and biomarker for cell division cycle 37 like 1.

Conclusion

CD37L1 is a 14-kDa protein that is predominantly localized to the nucleus during the S phase of the CDC. It functions as a cochaperone for the HSP90 dimeric form during the S phase of the CDC. CD37L1 has been shown to play a role in the regulation of cell cycle progression, cell survival, and cell adhesion. As a result, CD37L1 is a promising drug target and biomarker for cell division cycle 37 like 1. Further studies are needed to fully understand its functions in the CDC and its potential as a drug.

Protein Name: Cell Division Cycle 37 Like 1, HSP90 Cochaperone

Functions: Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90

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