Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins.

BZIP domain-containing protein.

Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins.

Transitional endoplasmic reticulum ATPase homolog 2; ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates. However, able to prevent aggregation of unfolded proteins also in an ATP-independent manner. Targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains. Involved in the cytoplasmic elimination of misfolded proteins exported from the ER. This pathway, known as ERAD, prevents [...]

Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins.

Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...]

Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins.

Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.

Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins.

Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family.

Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins.

Suppressor/Enhancer of Lin-12.

Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins.

E3 ubiquitin-protein ligase hrd-1; Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated ubc-7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system, which is also called the ER-associated degradation (ERAD) system, involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins. Protects cells from ER stress-induced apoptosis. Thought to play [...]

Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins.

UBX domain-containing protein 4; Probably acts as an adapter for ATPase cdc-48.1 and/or cdc- 48.2, conferring substrate specificity. May play a role in the ER- associated protein degradation pathway (ERAD) possibly acting as a platform to recruit both ubql-1 and cdc-48.1 and/or cdc-48.2 to the ER during ERAD.

Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins.

BZIP domain-containing protein.

Signal peptidase complex catalytic subunit SEC11.

TAZ-type domain-containing protein.

Phosphatidylinositol 3-kinase age-1; Phosphatidylinositol 3-kinase homolog that regulates longevity and diapause. Promotes cell survival during embryonic development by recruiting akt-1/2 to the plasma membrane through the production of PtdIns(3,4,5)P3. Could function in the development or neuroendocrine signaling of the dauer pathway. Mediates susceptibility to enteropathogenic E.coli infection. May negatively regulate AYI interneuron neurite outgrowth. Plays a role in aversive olfactory learning when an odor is associated with food deprivation. Regulates this process by promoting the [...]

Forkhead box protein O; Forkhead-type transcription factor. Binds to the promoters of genes that contain the daf-16 binding element (DBE), TTGTTTAC, in their regulatory region. Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway which affects lipogenesis, lifespan, starvation survival, heat shock and oxidative stress responses, and dauer formation. Longevity signaling predominantly arises from expression in the intestine. Daf-16 transcriptional activity is negatively regulated by cytoplasmic sequestration by association with ftt-2. Inhibition is required for the carbon [...]

Phosphatidylinositol 3-kinase age-1; Phosphatidylinositol 3-kinase homolog that regulates longevity and diapause. Promotes cell survival during embryonic development by recruiting akt-1/2 to the plasma membrane through the production of PtdIns(3,4,5)P3. Could function in the development or neuroendocrine signaling of the dauer pathway. Mediates susceptibility to enteropathogenic E.coli infection. May negatively regulate AYI interneuron neurite outgrowth. Plays a role in aversive olfactory learning when an odor is associated with food deprivation. Regulates this process by promoting the [...]

Insulin-like receptor subunit alpha; Insulin receptor-like tyrosine kinase which regulates metabolism, controls longevity and prevents developmental arrest at the dauer stage. Binding of INS family members may either stimulate, or antagonize, association of the receptor with downstream mediators such as pdk-1 and age-1. Required for germline progenitor proliferation during larval development. Required for the response to environmental stimuli such as food, pheromone, and temperature. Negatively regulates resistance to UV and oxidative stress. Role in immune function and pathogen resist [...]

Phosphatidylinositol 3-kinase age-1; Phosphatidylinositol 3-kinase homolog that regulates longevity and diapause. Promotes cell survival during embryonic development by recruiting akt-1/2 to the plasma membrane through the production of PtdIns(3,4,5)P3. Could function in the development or neuroendocrine signaling of the dauer pathway. Mediates susceptibility to enteropathogenic E.coli infection. May negatively regulate AYI interneuron neurite outgrowth. Plays a role in aversive olfactory learning when an odor is associated with food deprivation. Regulates this process by promoting the [...]

Protein glp-1; Involved in the specification of the cell fates of the blastomeres, ABa and APa. Proper signaling by glp-1 induces ABa descendants to produce anterior pharyngeal cells, and APa descendants to adopt a different fate. Contributes to the establishment of the dorsal-ventral axis in early embryos. Regulates germ cell mitotic proliferation probably by regulating MAP kinase phosphatase lip-1 expression. Plays a negative role in lifespan.

Phosphatidylinositol 3-kinase age-1; Phosphatidylinositol 3-kinase homolog that regulates longevity and diapause. Promotes cell survival during embryonic development by recruiting akt-1/2 to the plasma membrane through the production of PtdIns(3,4,5)P3. Could function in the development or neuroendocrine signaling of the dauer pathway. Mediates susceptibility to enteropathogenic E.coli infection. May negatively regulate AYI interneuron neurite outgrowth. Plays a role in aversive olfactory learning when an odor is associated with food deprivation. Regulates this process by promoting the [...]

HSF_DOMAIN domain-containing protein.

Phosphatidylinositol 3-kinase age-1; Phosphatidylinositol 3-kinase homolog that regulates longevity and diapause. Promotes cell survival during embryonic development by recruiting akt-1/2 to the plasma membrane through the production of PtdIns(3,4,5)P3. Could function in the development or neuroendocrine signaling of the dauer pathway. Mediates susceptibility to enteropathogenic E.coli infection. May negatively regulate AYI interneuron neurite outgrowth. Plays a role in aversive olfactory learning when an odor is associated with food deprivation. Regulates this process by promoting the [...]

Stress-activated protein kinase jnk-1; Serine/threonine-protein kinase which responds to activation by environmental stress by phosphorylating a number of transcription factors such as daf-16, and thus regulates transcriptional activity. By phosphorylating daf-16, plays a role in daf-16 nuclear translocation in intestinal cells in response to environmental stresses such as heat and oxidative stresses. Downstream of jkk-1, may coordinate locomotion via type-D GABAergic motoneurons and regulates synaptic vesicle transport in conjunction with unc-16. Independently of jkk-1, may regulate s [...]

BZIP domain-containing protein.

Derlin-2; May be required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Its precise function remains unclear, but its ability to complement der1 mutations in C.cerevisiae, suggests a similar function in the degradation of ER misfolded proteins.

BZIP domain-containing protein.

Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...]

BZIP domain-containing protein.

Forkhead box protein O; Forkhead-type transcription factor. Binds to the promoters of genes that contain the daf-16 binding element (DBE), TTGTTTAC, in their regulatory region. Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway which affects lipogenesis, lifespan, starvation survival, heat shock and oxidative stress responses, and dauer formation. Longevity signaling predominantly arises from expression in the intestine. Daf-16 transcriptional activity is negatively regulated by cytoplasmic sequestration by association with ftt-2. Inhibition is required for the carbon [...]

BZIP domain-containing protein.

Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.

BZIP domain-containing protein.

Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family.