MITF (Microphthalmia-associated transcription factor )
Transcription Factors

DEFINITION

Microphthalmia-associated transcription factor/ MITF also known as class E basic helix-loop-helix protein 32 or bHLHe32 is a protein that in humans is encoded by the MITF gene.

MITF is a basic helix-loop-helix leucine zipper transcription factor involved in lineage-specific pathway regulation of many types of cells including melanocytes, osteoclasts, and mast cells, cells with a prominent role of lysosomes.

THE GENE

Database	Link
HGNC	MITF
Uniprot	MITF_HUMAN

• H-InvDB
• QuickGO
• Reactome
• Wikigenes includes links to
  • NCBI
  • NCBI SNP
  • iHOP resource
  • OMIM
  • UniProt
  • Ensembl
  • HGNC

CHEMICAL STRUCTURE AND IMAGES

When relevant for the function

• Primary structure
• Secondary structure
• Tertiary structure
  • PDB
• Quaternary structure

Protein Aminoacids Percentage
The Protein Aminoacids Percentage gives useful information on the local environment and the metabolic status of the cell (starvation, lack of essential AA, hypoxia)

Protein Aminoacids Percentage (Width 700 px)

SYNTHESIS AND TURNOVER

mRNA synthesis
protein synthesis

post-translational modifications
degradation

CELLULAR FUNCTIONS

cellular localization,
biological function

• Enzymes

Database	Link
BRENDA - The Comprehensive Enzyme Information System	"URL":
KEGG Pathways	"URL":
Human Metabolome Database	"URL":

• Cell signaling and Ligand transport
• Structural proteins

REGULATION

DIAGNOSTIC USE

mtor+and+MITF

alternativi

MITF invasion

MITF+and+respiratory+chain

mitf+and+diet

Fish oil suppresses bone resorption by inhibiting osteoclastogenesis through decreased expression of M-CSF, PU.1, MITF and RANK in ovariectomized rats. 2913

• Abstract »
  Dietary fish oil suppressed ovariectomy‑stimulated osteoclastogenesis by inhibiting the expression of M‑CSF, PU.1, MITF and RANK in the early stages of osteoclastogenesis, upstream of RANKL signaling.

mitf+downregulation

Regulation of mTORC1 by Small GTPases in Response to Nutrients. 2020

• Abstract
  Mechanistic target of rapamycin complex 1 (mTORC1) is a highly evolutionarily conserved serine/threonine kinase that regulates cell growth and metabolism in response to multiple environmental cues, such as nutrients, hormones, energy, and stress. Deregulation of mTORC1 can lead to diseases such as diabetes, obesity, and cancer. A series of small GTPases, including Rag, Ras homolog enriched in brain (Rheb), adenosine diphosphate ribosylation factor 1 (Arf1), Ras-related protein Ral-A, Ras homolog (Rho), and Rab, are involved in regulating mTORC1 in response to nutrients, and mTORC1 is differentially regulated via these small GTPases according to specific conditions. Leucine and arginine sensing are considered to be well-confirmed amino acid-sensing signals, activating mTORC1 via a Rag GTPase-dependent mechanism as well as the Ragulator complex and vacuolar H+-adenosine triphosphatase (v-ATPase). Glutamine promotes mTORC1 activation via Arf1 independently of the Rag GTPase. In this review, we summarize current knowledge regarding the regulation of mTORC1 activity by small GTPases in response to nutrients, focusing on the function of small GTPases in mTORC1 activation and how small GTPases are regulated by nutrients.