Autophagy

The Beclin 1 protein is a central regulator of autophagy in mammalian cells. Autophagy is an essential process used to maintain cellular homeostasis by degrading and recycling cellular components such as damaged or worn out organelles and macromolecules. Autophagy is also activated in response to cellular stresses such as nutrient starvation or intracellular pathogens and can protect the cell from programmed cell death.

ATG9A is the only essential integral membrane protein involved in autophagy. ATG9A contains six transmembrane domains and initiates the assembly of autophagosomes. The autophagosome is a double-membrane structure that engulfs and eventually degrades cytoplasmic materials such as organelles or macromolecules. Assembly of the autophagosome requires the delivery of lipids and membrane components to initiate and expand the double-membrane pre-autophagosome structure called the isolation membrane.

Bcl-2 nineteen-kilodalton interacting protein 3 (BNIP3) is a pro-apoptotic BH3-only protein. BNIP3 localizes to the mitochondrial membrane where it plays a key role in mitochondrial autophagy and cell death pathways. Similar to other Bcl-2 family members, BNIP3 binds to Bcl-2 and can activate the downstream effectors of Bax/Bak.

Autophagy, a protein degradation process through autophagosome-lysosomal pathway, is important for cellular homeostasis and plays a role in many diseases. To help researchers learn more about this process and the products available for its study, Novus Biologicals has released a new Autophagy catalog.

The BAG proteins are a large family of chaperone regulators governing a wide range of cell processes such as proliferation, survival, stress response, tumorigenesis, neuronal differentiation, growth arrest and apoptosis as reviewed in Takayama et al¹. BAG proteins are co-chaperones that interact with several forms of the chaperone heat shock protein 70 (Hsp70) – the association allows them to both positively and negatively regulate Hsp70.

PINK1 (PTEN induced putative kinase 1) is a mitochondrial serine/threonine kinase which maintains mitochondrial function/integrity, provides protection against mitochondrial dysfunction during cellular stress, potentially by phosphorylating mitochondrial proteins, and is involved in the clearance of damaged mitochondria via selective autophagy (mitophagy).

The ATG5 protein belongs to the ATG autophagy regulator family. This family controls the highly conserved cell's homeostatic response to a wide variety of both self- and foreign-originating cellular stimuli. ATG5 itself is ubiquitously expressed in most cells and most often found co-localized with the cytoplasmic non-muscle actin protein under normal resting conditions. Upon activation of apoptosis, ATG5 expression is then dramatically intensified, with ATG5 directly complexing with its ATG family members to produce autophagosomes.

LAMP2 belongs to the family of membrane glycoproteins who confer selectins with carbohydrate ligands. LAMP2 has been implicated in tumor cell metastasis, as well as overall protection, maintenance, and adhesion of the lysosome. It appears that LAMP2 may protect the lysosomal membrane from autophagy, as well as maintain the required acidic environment necessary for proper function.  LAMP2 is a single-pass type I membrane protein that shuttles between endosomes, lysosomes, and the plasma membrane.

ATG5, or Autophagy Related 5, is a protein crucial for autophagy. Autophagy is a mechanism in which dysfunctional or pathogenic cells or cellular components are degraded and sometimes recycled. This process happens when ATG5 conjugates with another protein and associates with a cup shaped isolation membrane.

APE1 is involved in repairing oxidative DNA damages in vitro, regulates the redox of transcriptional factors, repairs AP sites in DNA, and is important for embryonic development in mice. Learn more about APE1 in our infographic below.

Novus Biologicals offers APE1 reagents for your research needs including: