Gene localization and developmental expression of light chain 3: A common subunit of microtubule-associated protein 1A (MAP1A) and MAP1B

Mann, Sukhdeep Kaur; Hammarback, James A.

doi:10.1002/(sici)1097-4547(19960301)43:5<535::aid-jnr3>3.0.co;2-j

Cited by 50 publications

(25 citation statements)

References 22 publications

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“…GABARAPL1 shows 87% identity with GABARAP and 61% identity with GATE-16 5,6 and also shares a distant homology with LC3A (30.8% identity), LC3B (29% identity) and LC3C (35.8% identity). [7][8][9][10] Members of the GABARAP and LC3 families are composed of 117 to 145 amino acids and all possess a conserved C-terminal glycine, essential for their role in autophagy (Fig. 1).…”

Section: The Gabarap Familycontrasting

confidence: 91%

GABARAPL1 (GEC1): Original or copycat?

Grand

Chakrama²,

Seguin-Py³

et al. 2011

Autophagy

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Section: The Gabarap Familycontrasting

confidence: 91%

GABARAPL1 (GEC1): Original or copycat?

Grand

Chakrama²,

Seguin-Py³

et al. 2011

Autophagy

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“…TP53INP1s were precipitated with a streptavidin-containing resin and the presence of GABARAP-YFP or GABARAPL2-YFP in the precipitate was monitored by western blot (Figure 1b). As these proteins are members of a structurally and functionally related multigenic family (mammalian homologs of ATG8), which also include LC3, 23 we also assessed by the same strategy that TP53INP1a and b interact with transfected and endogenous LC3 (Figure 1c). To check whether interaction between TP53INP1s with GABARAP, GABARAPL2 and LC3 occurred in living cells we performed a Bioluminescence Resonance Energy Transfer (BRET) assay, which allows the real-time detection of protein-protein interactions.…”

Section: Resultsmentioning

confidence: 99%

TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death

et al. 2012

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TP53INP1 (tumor protein 53-induced nuclear protein 1) is a tumor suppressor, whose expression is downregulated in cancers from different organs. It was described as a p53 target gene involved in cell death, cell-cycle arrest and cellular migration. In this work, we show that TP53INP1 is also able to interact with ATG8-family proteins and to induce autophagy-dependent cell death. In agreement with this finding, we observe that TP53INP1, which is mainly nuclear, relocalizes in autophagosomes during autophagy where it is eventually degraded. TP53INP1-LC3 interaction occurs via a functional LC3-interacting region (LIR). Inactivating mutations of this sequence abolish TP53INP1-LC3 interaction, relocalize TP53INP1 in autophagosomes and decrease TP53INP1 ability to trigger cell death. Interestingly, TP53INP1 binds to ATG8-family proteins with higher affinity than p62, suggesting that it could partially displace p62 from autophagosomes, modifying thereby their composition. Moreover, silencing the expression of autophagy related genes (ATG5 or Beclin-1) or inhibiting caspase activity significantly decreases cell death induced by TP53INP1. These data indicate that cell death observed after TP53INP1-LC3 interaction depends on both autophagy and caspase activity. We conclude that TP53INP1 could act as a tumor suppressor by inducing cell death by caspasedependent autophagy. Increased resistance to cell death participates in pancreatic cancer progression. Cells unable to undergo self elimination accumulate mutations and epigenetic modifications that in turn induce uncontrolled replication. 1 Various concomitant mechanisms exist in normal cells to induce death and, as consequence, a number of known cell-death regulators are missing in cancer cells. One of the most studied is the tumor suppressor TP53, which is inactivated in 450% of pancreatic tumors. 2 p53 induces cell death by both direct permeabilization of the outer mitochondrial membrane or translocation to the nucleus where it activates the transcription of several target genes. One of the p53 target genes is TP53INP1 (tumor protein 53-induced nuclear protein 1). 3-6 p53-dependent expression of TP53INP1 is triggered in response to several stress agents such as mutagens, ethanol, heat shock or conditions promoting reactive oxygen species formation (i.e., exposure to UV light or g-irradiation). 4,6 TP53INP1 interacts with kinases, HIPK2 and PKCd, which in turn phosphorylate p53 creating a positive feedback loop between p53 and TP53INP1. 7,8 Our laboratory demonstrated that TP53INP1 is a tumor suppressor on the basis of the following observations: (i) TP53INP1 deficient mice present with an increased susceptibility to tumor development; (ii) TP53INP1 is lost at very early stages of pancreatic carcinogenesis through a mechanism involving the oncogenic miR-155 microRNA and (iii) when TP53INP1 expression is restored in pancreatic cells, it suppresses xenograft growth by increasing apoptotic cell death through a caspase-dependent mechanism. 3,9,10 More recently, in an attempt t...

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“…78 In summary, the process of neurite formation involves several structures including the cytoskeleton, and some of its component parts such as microfilaments, microtubules, MAPs like MAP1, MAP2 and tau. This process appears to be highly regulated with a machinery that we are just beginning to understand.…”

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confidence: 99%

New genes associated with schizophrenia in neurite formation: a review of cell culture experiments

Bellon

2007

Mol Psychiatry

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New genes consistently associated with schizophrenia include NRG1, Akt, DISC-1 and dysbindin-1. Since these genes participate in neurotransmission, neuroplasticity and neurodevelopment it has not been easy to elucidate which of these roles are abnormal in patients with schizophrenia. Neurite formation is identified as a crucial stage in development, and it is proposed that a defect in neurite formation originating from abnormally encoded proteins by these new genes could be at least an in vitro marker that reflects the most consistent molecular and neuroanatomical findings in schizophrenia. A systematic review of the literature linking the process of neurite formation to genes with replicated evidence that supported their association with schizophrenia was conducted. In addition, an outline of the process of neurite formation was included. Neurite formation was shown to be induced by neuregulins, the product of the gene NRG1. The activation of Akt, a serine/threonine kinase, promoted neurite formation in six independent studies. Conversely, two studies found that Akt inhibits neurite outgrowth. Stronger evidence supporting an association with the new genes related to schizophrenia and neurite formation comes from DISC-1. Defects in DISC-1 protein were shown to directly alter the process of neurite formation. Dysbindin-1 has not yet been directly implicated in neurite outgrowth. These findings suggest that the proteins encoded by NRG1, Akt and DISC-1 are implicated in the process of neurite formation in cellular models as well as, at least in part, animal models during development. Abnormalities in this process could have potential etiologic implications for schizophrenia. Direct evidence, however, of abnormal neurite formation in patients with schizophrenia is still missing. Limitations to this model are identified.

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Gene localization and developmental expression of light chain 3: A common subunit of microtubule-associated protein 1A (MAP1A) and MAP1B

Cited by 50 publications

References 22 publications

GABARAPL1 (GEC1): Original or copycat?

GABARAPL1 (GEC1): Original or copycat?

TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death

New genes associated with schizophrenia in neurite formation: a review of cell culture experiments

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