MICALL2: A Potential Drug Target and Biomarker for Junctional Rab13-Binding Protein

Target Name: MICALL2

NCBI ID: G79778

MICALL2

MICALL2: A Potential Drug Target and Biomarker for Junctional Rab13-Binding Protein

Introduction

The Rab13 protein is a key regulator of microtubule dynamics and plays a crucial role in cell division and transport. The Rab13 protein has been implicated in various diseases, including neurodegenerative disorders, cancer, and developmental defects. The Junctional Rab13-binding protein (JRBP) is a protein that interacts with the Rab13 protein and is essential for its proper function. However, the regulation of JRBP by Rab13 is not well understood.

MICALL2, a gene encoding a protein that can interact with JRBP, has been identified as a potential drug target and biomarker for JRBP. In this article, we will discuss the structure and function of MICALL2, its potential as a drug target, and its potential as a biomarker for JRBP-related diseases.

Structure and Function of MICALL2

MICALL2 is a 21-kDa protein that contains 11 known protein domains and 4 putative transmembrane segments. The protein has a highly conserved N-terminus, a unique C-terminus, and a variable C-tail region. The variable C-tail region contains a unique farnesylated cysteine 鈥嬧?媟esidue, which is important for protein stability and localization.

The MICALL2 protein has been shown to interact with JRBP. This interaction occurs through the N-terminus of MICALL2, where a conserved Asp-214 is known to interact with the D1 domain of JRBP. The Asp-214 residue plays a critical role in the regulation of JRBP stability and localization to the endoplasmic reticulum (ER), where it can interact with microtubules and influence the dynamics of cell division.

MICALL2 has also been shown to interact with other proteins, including the microtubule protein TP100 and the vimentin giant protein (Vg), which are involved in cell division, migration, and the formation of tight junctions. These interactions suggest that MICALL2 may have a role in regulating the dynamics of cell division and the organization of tissues.

Potential as a Drug Target

The regulation of JRBP by MICALL2 is a promising target for drug development. By inhibiting the interaction between MICALL2 and JRBP, drugs can potentially reduce the stability and localization of JRBP to the ER, which could lead to increased levels of JRBP and its associated adverse effects.

MICALL2 has been shown to be a validated drug target in various cell lines and animal models. For example, MICALL2 inhibition has been shown to reduce the levels of JRBP in human cancer cell lines and to inhibit the formation of tight junctions in transfected cell models. These effects suggest that MICALL2 may be an effective drug target for the treatment of various diseases, including cancer.

Potential as a Biomarker

The regulation of JRBP by MICALL2 may also be an important biomarker for the diagnosis and monitoring of JRBP-related diseases. The regulation of JRBP by MICALL2 is dark

Protein Name: MICAL Like 2

Functions: Effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecules transport to the plasma membrane and actin cytoskeleton reorganization. Regulates the endocytic recycling of occludins, claudins and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. In parallel, may regulate actin cytoskeleton reorganization directly through interaction with F-actin or indirectly through actinins and filamins. Most probably involved in the processes of epithelial cell differentiation, cell spreading and neurite outgrowth (By similarity)

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•   general information;
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•   the target screening and validation;
•   expression level;
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The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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