Pleckstrin Homology Domain Containing N1: Critical Role in Cellular Processes

Target Name: PLEKHN1

NCBI ID: G84069

Other Name(s): Pleckstrin homology domain containing N1, transcript variant 2 | PLEKHN1 variant 2 | CLPABP | Pleckstrin homology domain-containing family N member 1 (isoform b) | RP11-54O7.7 | PH domain-containing family N member 1 | Cardiolipin and phosphatidic acid-binding protein | pleckstrin homology domain-containing family N member 1 | Pleckstrin homology domain-containing family N member 1 (isoform a) | PLEKHN1 variant 1 | Pleckstrin homology domain-containing family N member 1 | Pleckstrin homology domain containing N1, transcript variant 1 | PKHN1_HUMAN | cardiolipin and phosphatidic acid-binding protein | pleckstrin homology domain containing N1

Pleckstrin Homology Domain Containing N1: Critical Role in Cellular Processes

Pleckstrin homology domain containing N1 (Pleckstrin homology domain containing N1, transcript variant 2) is a protein that plays a critical role in various cellular processes. It is a protein that is expressed in many different tissues and organs, including brain, heart, liver, and muscle. Its function is to help regulate the movement of cells and to maintain the structure of various cell organelles.

Pleckstrin homology domain containing N1 is a protein that contains a unique domain that is composed of multiple amino acids that are similar to those of the protein tyrosine kinase (TK). This domain is known as the Pleckstrin homology domain, and it is a key part of the protein's structure and function.

One of the key functions of Pleckstrin homology domain containing N1 is its role in cell signaling. This protein is involved in a variety of signaling pathways, including the regulation of cell growth, differentiation, and survival. It is also involved in the regulation of cell-cell interactions and in the formation of various cellular structures.

Another important function of Pleckstrin homology domain containing N1 is its role in the regulation of protein function. This protein helps to regulate the activity of other proteins, and it is also involved in the degradation of certain proteins that are no longer needed.

Pleckstrin homology domain containing N1 is also involved in the regulation of cellular transport. This protein helps to regulate the movement of proteins and other molecules into and out of cells, and it is also involved in the regulation of the movement of vesicles within cells.

In addition to its role in cell signaling and regulation, Pleckstrin homology domain containing N1 is also involved in the regulation of cellular structure. This protein helps to regulate the structure and organization of various cellular organelles, including the mitochondria and the endoplasmic reticulum.

Pleckstrin homology domain containing N1 is also involved in the regulation of cellular processes related to the cytoskeleton. This protein helps to regulate the movement of chromosomes within cells, and it is also involved in the regulation of the cytoskeleton itself.

In conclusion, Pleckstrin homology domain containing N1 is a protein that plays a critical role in various cellular processes. Its function is to help regulate the movement of cells, to maintain the structure of various cell organelles, and to participate in the regulation of cell signaling, protein function, and cellular structure. Given its involvement in these critical processes, Pleckstrin homology domain containing N1 is a potential drug target and a biomarker for a variety of diseases.

Protein Name: Pleckstrin Homology Domain Containing N1

Functions: Controls the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR, in cooperation with the RNA stabilizer ELAVL1 (PubMed:29180010). Decreases the stability of the leptin mRNA by antagonizing the function of ELAVL1 by inducing its atypical recruitment from the nucleus to the cytosol (By similarity). Binds to cardiolipin (CL), phosphatidic acid (PA), phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidylserine (PS) (PubMed:18191643). Promotes apoptosis by enhancing BAX-BAK hetero-oligomerization via interaction with BID in colon cancer cells (PubMed:29531808) (By similarity)

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