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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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Related Experiment Video

Updated: May 7, 2026

Characterization of MLKL-mediated Plasma Membrane Rupture in Necroptosis
08:55

Characterization of MLKL-mediated Plasma Membrane Rupture in Necroptosis

Published on: August 7, 2018

MLL becomes functional through intra-molecular interaction not by proteolytic processing.

Akihiko Yokoyama1, Francesca Ficara, Mark J Murphy

  • 1Laboratory for Malignancy Control Research, Kyoto University Graduate School of Medicine, Kyoto, Japan.

Plos One
|September 17, 2013
PubMed
Summary
This summary is machine-generated.

Intra-molecular complex formation is essential for mixed lineage leukemia (MLL) protein function in embryonic development and hematopoietic progenitor proliferation. Proteolytic cleavage of MLL is dispensable for these processes in vivo.

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Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis
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Related Experiment Videos

Last Updated: May 7, 2026

Characterization of MLKL-mediated Plasma Membrane Rupture in Necroptosis
08:55

Characterization of MLKL-mediated Plasma Membrane Rupture in Necroptosis

Published on: August 7, 2018

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis
08:55

Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis

Published on: October 28, 2016

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Hematopoiesis

Background:

  • The mixed lineage leukemia (MLL) protein regulates hematopoietic progenitor proliferation and is implicated in leukemogenesis.
  • MLL protein maturation involves intra-molecular complex formation and proteolytic cleavage, but their in vivo significance is unknown.

Purpose of the Study:

  • To investigate the in vivo roles of MLL intra-molecular complex formation and proteolytic cleavage in MLL protein function.
  • To determine the necessity of these post-transcriptional modifications for MLL-dependent gene activation and hematopoietic progenitor proliferation.

Main Methods:

  • Generation of mouse mutant alleles expressing MLL variants incapable of intra-molecular interaction (de) or resistant to cleavage (uc).
  • Analysis of embryonic development, hematopoietic progenitor numbers, and MLL target gene expression in homozygous mutant mice and fibroblasts.

Main Results:

  • Homozygous de mice exhibited embryonic lethality, developmental failure, and reduced hematopoietic progenitors.
  • Homozygous uc mice showed no apparent developmental defects.
  • MLL target gene expression was severely impaired in de fibroblasts but normal in uc fibroblasts.

Conclusions:

  • Intra-molecular complex formation is a critical maturation step for MLL protein function in vivo.
  • Proteolytic cleavage of MLL is not essential for its role in gene activation and proliferation during embryonic development and hematopoiesis.