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Menin localization in cell membrane compartment.

Xin He¹, Lei Wang^1,2, Jizhou Yan³

¹a Abramson Family Cancer Research Institute, Department of Cancer Biology, Abramson Cancer Center, University of Pennsylvania Perelman School of Medicine , 421 Curie Blvd., Philadelphia , PA 19104 , USA.

Cancer Biology & Therapy

|November 13, 2015

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Menin protein, encoded by the MEN1 gene, associates with the cell membrane, potentially via serine palmitoylation. It also resides within membrane vesicles, suggesting novel roles beyond its nuclear functions.

Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Menin, encoded by the MEN1 gene, is a nuclear protein with tumor suppressor roles in endocrine organs and oncogenic functions in leukemia.
Menin acts as a scaffold protein, regulating gene transcription through interactions with various partners in the nucleus.
The extranuclear functions of menin, particularly its association with the cell membrane, are not well understood.

Purpose of the Study:

To investigate the localization and association of menin with the cell membrane.
To elucidate the mechanism by which menin interacts with the cell membrane.

Main Methods:

Cellular fractionation to isolate membrane components.
Serine palmitoylation assays.
Proteolysis assays using trypsin.

Keywords:

Cell membrane menin palmitoylation secretory pathway

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Detergent treatment to disrupt membrane structures.

Cellular staining and microscopy.

Main Results:

A small fraction of menin was found to associate with the cell membrane, likely through serine palmitoylation.
Membrane-associated menin showed resistance to trypsin digestion, suggesting localization within membrane vesicles.
Disruption of membrane structures with detergent abolished menin detection at the membrane.
Cellular staining revealed menin in the cell membrane and punctate organelles.

Conclusions:

Menin peripherally associates with the cell membrane and resides within intracellular membrane vesicles.
These findings reveal novel extranuclear roles for menin, expanding our understanding of its cellular functions.