RACK1: A protein Target for Cancer and Neurodegenerative Disorders

Target Name: RACK1

NCBI ID: G10399

RACK1

Other Name(s): guanine nucleotide-binding protein subunit beta-like protein 12.3 | small ribosomal subunit protein RACK1 | uman lung cancer oncogene 7 protein | Receptor for activated C kinase | cell proliferation-inducing gene 21 protein | Guanine nucleotide-binding protein beta subunit-like protein 12.3 | Guanine nucleotide-binding protein subunit beta-like protein 12.3 | Protein homologous to chicken B complex protein, guanine nucleotide binding | lung cancer oncogene 7 | receptor of activated protein kinase C 1 | Receptor of activated protein kinase C 1 | PIG21 | protein homologous to chicken B complex protein, guanine nucleotide binding | H12.3 | Guanine nucleotide-binding protein subunit beta-2-like 1 | human lung cancer oncogene 7 protein | guanine nucleotide binding protein (G protein), beta polypeptide 2-like 1 | GNB2L1 | RACK1_HUMAN | Gnb2-rs1 | Lung cancer oncogene 7 | HLC-7 | Cell proliferation-inducing gene 21 protein | guanine nucleotide-binding protein subunit beta-2-like 1 | Receptor of activated protein C kinase 1 | Proliferation-inducing gene 21 | Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed | receptor for activated C kinase 1 | Human lung cancer oncogene 7 protein | Receptor of activated protein C kinase 1, N-terminally processed | guanine nucleotide binding protein beta polypeptide 2-like 1 | proliferation-inducing gene 21 | Receptor for activated C kinase 1 | Guanine nucleotide binding protein (G protein), beta polypeptide 2-like 1 | Small ribosomal subunit protein RACK1

RACK1: A protein Target for Cancer and Neurodegenerative Disorders

Introduction

RACK1 (Guanine Nucleotide-Binding Protein Subunit Beta-Like Protein 12.3) is a unique protein that has caught the attention of researchers due to its various roles in various biological processes. It is a member of the RACK family of proteins, which are known to play a crucial role in regulating various cellular processes. RACK1 is a 12.3 kDa protein that is expressed in most tissues and cells in the human body.

The RACK family of proteins was first identified based on its ability to interact with guanine nucleotides, which are the genetic units that carry genetic information in DNA. These interactions led to the conclusion that RACK proteins might play a role in regulating gene expression and cell signaling . Subunit beta-like protein 12.3, specifically, has been shown to interact with guanine nucleotides and regulate various cellular processes, including cell adhesion, migration, and invasion.

Despite its potential role in cellular signaling, RACK1 is still an unexplored protein. There is limited research on its functions and potential drug targets. However, recent studies have suggested that RACK1 may be a promising drug target for cancer and neurodegenerative disorders. In this article , we will explore the biology and potential drug targets of RACK1 in greater detail.

The RACK1 Protein

RACK1 is a member of the RACK family of proteins, which are known to be involved in various cellular processes, including cell signaling, gene regulation, and protein-protein interactions. These proteins are characterized by a conserved catalytic core and a unique N-terminal region that contains a putative RNA binding structure (PBS) domain.

The N-terminal region of RACK1 contains a 126 amino acid residue that includes several conserved domains, including a leucine-rich repeat (LRR), a conserved protein-protein interaction (PPI), and a putative RNA binding structure (PBS). The LRR is a common structural motif that is found in various proteins, including DNA-binding proteins, and is known to play a role in protein-protein interactions. The PPI domain is a conserved region that is found in proteins that interact with RNA, including RACK1. The BSG-ASN-PBS domain is a unique structure that is found in RACK1 and is known to be involved in protein-protein interactions.

Expression and Localization

RACK1 is expressed in most tissues and cells in the human body, including muscle, pancreas, and brain. It is also expressed in various types of cancer, including breast, ovarian, and colorectal cancer. RACK1 has been shown to localize to the endoplasmic reticulum (ER) and to be predominantly expressed in the cytoplasm.

Functions and Interactions

Several studies have suggested that RACK1 plays a role in regulating various cellular processes, including cell adhesion, migration, and invasion. RACK1 has been shown to interact with various proteins, including the transcription factor NF-kappa-B and the protein Src. These interactions may play a role in regulating the expression of genes that are involved in cell signaling and differentiation.

In addition to its role in cell signaling, RACK1 has also been shown to be involved in the regulation of cell adhesion. RACK1 has been shown to interact with the adhesion molecule E-cadherin and to regulate its trafficking to the plasma membrane. This suggests that RACK1 may play a role in the regulation of cell-cell adhesion and the development of various types of cancer.

Furthermore, RACK1 has also been shown to be involved in the regulation of cell migration and invasion. It has been shown to interact with the protein vimentin and to regulate its localization to the plasma

Protein Name: Receptor For Activated C Kinase 1

Functions: Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:23636399). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (PubMed:28132843). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157). Promotes migration of breast carcinoma cells by binding to and activating RHOA (PubMed:20499158). Acts as an adapter for the dephosphorylation and inactivation of AKT1 by promoting recruitment of PP2A phosphatase to AKT1 (By similarity)

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