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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
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,...
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Energy to Drive Translocation01:37

Energy to Drive Translocation

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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Immunoglobulin-like Cell Adhesion Molecules01:31

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

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Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
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Multiple myeloma immunoglobulin lambda translocations portend poor prognosis.

Benjamin G Barwick1,2,3, Paola Neri4, Nizar J Bahlis4

  • 1Department of Hematology and Medical Oncology, Emory University School of Medicine, 1365 Clifton Rd. NE, Atlanta, GA, 30322, USA.

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New research reveals immunoglobulin lambda (IgL) translocations in multiple myeloma indicate poor prognosis. These IgL translocations may cause resistance to therapies like IMiDs, potentially misclassifying high-risk patients.

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Area of Science:

  • Hematology
  • Cancer Genomics
  • Molecular Biology

Background:

  • Multiple myeloma is a plasma cell malignancy with a 20% high-risk group experiencing poor outcomes.
  • Current therapies benefit most patients, but a significant subset faces relapse or mortality within two years.

Purpose of the Study:

  • To investigate the role of structural variants, specifically translocations involving the immunoglobulin lambda (IgL) locus, in newly-diagnosed multiple myeloma.
  • To determine the prognostic significance and potential therapeutic implications of IgL translocations.

Main Methods:

  • Analysis of structural variants from 795 newly-diagnosed multiple myeloma patients in the CoMMpass study.
  • Correlation of IgL translocations with patient prognosis, genetic features, and response to therapies.

Main Results:

  • Translocations involving the IgL locus were identified in 10% of patients and associated with poor prognosis.
  • IgL-MYC translocations, often co-occurring with enhancer amplifications and hyperdiploid disease, were particularly linked to adverse outcomes.
  • Patients with IgL translocations showed resistance to IMiD therapies, which target the transcription factor IKZF1 that binds the IgL enhancer.

Conclusions:

  • IgL translocations, especially IgL-MYC, represent a driver of poor prognosis in multiple myeloma.
  • The co-occurrence with hyperdiploid disease suggests IgL-MYC-translocated myeloma may be misclassified.
  • Resistance to IMiDs in IgL-translocated myeloma patients highlights a potential mechanism for therapeutic failure.