Cdc37 cDNA ORF clone, Rattus norvegicus(Norway rat)

Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.
Woodford MR, Sager RA, Marris E, Dunn DM, Blanden AR, Murphy RL, Rensing N, Shapiro O, Panaretou B, Prodromou C, Loh SN, Gutmann DH, Bourboulia D, Bratslavsky G, Wong M, Mollapour M
The EMBO journal36(24)3650-3665(2017 12)

Hsp90/Cdc37 assembly modulates TGF? receptor-II to act as a profibrotic regulator of TGF? signaling during cardiac hypertrophy.
Datta R, Bansal T, Rana S, Datta K, Chattopadhyay S, Chawla-Sarkar M, Sarkar S
Cellular signalling27(12)2410-24(2015 Dec)

Canonical and kinase activity-independent mechanisms for extracellular signal-regulated kinase 5 (ERK5) nuclear translocation require dissociation of Hsp90 from the ERK5-Cdc37 complex.
Erazo T, Moreno A, Ruiz-Babot G, Rodr?guez-Asiain A, Morrice NA, Espadamala J, Bayascas JR, G?mez N, Lizcano JM
Molecular and cellular biology33(8)1671-86(2013 Apr)

Hsp90-Cdc37 chaperone complex regulates Ulk1- and Atg13-mediated mitophagy.
Joo JH, Dorsey FC, Joshi A, Hennessy-Walters KM, Rose KL, McCastlain K, Zhang J, Iyengar R, Jung CH, Suen DF, Steeves MA, Yang CY, Prater SM, Kim DH, Thompson CB, Youle RJ, Ney PA, Cleveland JL, Kundu M
Molecular cell43(4)572-85(2011 Aug)

Blocking Hsp90-Cdc37 interactions during pressure overload hypertrophy results in ubiquitin-mediated proteasomal degradation of TGFBR2 leading to termination of TGF beta mediated signaling.
Title: Hsp90/Cdc37 assembly modulates TGF? receptor-II to act as a profibrotic regulator of TGF? signaling during cardiac hypertrophy.

C-terminal tail and determinants in the alphaE-helix of the catalytic domain allows the chaperones Hsp90 and Cdc37 to bind newly synthesized PKC beta II, a required event in the processing of PKC by phosphorylation
Title: The chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail.

CK2 activity was investigated both in vitro and in cultured cells by using anti-[pSer13]-Cdc37 antibody.
Title: Evaluating CK2 activity with the antibody specific for the CK2-phosphorylated form of a kinase-targeting cochaperone Cdc37.

CK2 and Cdc37 constitute a positive feedback machinery to control multiple Cdc37-dependent signaling protein kinases.
Title: CK2 binds, phosphorylates, and regulates its pivotal substrate Cdc37, an Hsp90-cochaperone.

Results unveil a regulatory mechanism of Cdc37, identify a molecular link between casein kinase 2 (CK2) and many crucial protein kinases via Cdc37, and reveal the molecular basis for the ability of CK2 to regulate pleiotropic cellular functions.
Title: CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37.