ADAM11

From WikiMD's medical encyclopedia


Overview

ADAM11 is a member of the ADAM (A Disintegrin and Metalloproteinase) family of proteins, which are involved in a variety of biological processes, including cell adhesion, cell fusion, and proteolysis. ADAM11 is encoded by the ADAM11 gene in humans and is known to play a role in the nervous system.

Structure

ADAM11 is a type I transmembrane protein that consists of several distinct domains:

  • A signal peptide that directs the nascent protein to the secretory pathway.
  • A pro-domain that is cleaved to activate the protein.
  • A metalloproteinase domain, although ADAM11 lacks proteolytic activity due to the absence of a critical zinc-binding motif.
  • A disintegrin domain that is involved in cell-cell and cell-matrix interactions.
  • A cysteine-rich domain and an EGF-like domain that may contribute to protein-protein interactions.
  • A transmembrane domain anchoring the protein to the cell membrane.
  • A cytoplasmic tail that may interact with intracellular signaling molecules.

Function

ADAM11 is primarily expressed in the nervous system, particularly in the brain. Although it lacks proteolytic activity, it is believed to play a role in cell adhesion and signaling. ADAM11 may be involved in the development and maintenance of the nervous system, influencing processes such as synapse formation and neuronal migration.

Clinical Significance

Mutations or alterations in the ADAM11 gene have been associated with neurological disorders. Research suggests that ADAM11 may be implicated in conditions such as epilepsy and certain neurodegenerative diseases. However, the exact mechanisms by which ADAM11 contributes to these conditions are still under investigation.

Research

Ongoing research is focused on understanding the precise role of ADAM11 in the nervous system and its potential involvement in neurological diseases. Studies are exploring the interactions of ADAM11 with other proteins and its impact on cellular signaling pathways.

Also see


ADAM Family

A Disintegrin and Metalloproteinase

Members
Functions
Related Topics
See Also



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Contributors: Prab R. Tumpati, MD