Related Experiment Video
Updated: Jul 27, 2025
05:28
Author Spotlight: Unveiling the Molecular Basis of Pain Perception and Neuropathic Pain
Published on: August 9, 2024
1.1K
iASPP regulates neurite development by interacting with Spectrin proteins.
Junhao Wang1, Chunhong Jia2, Qiong Gao1
1Fujian Key Laboratory for Translational Research in Cancer and Neurodegenerative Diseases, Institute for Translational Medicine, School of Basic Medical Sciences, Fujian Medical University, Fuzhou, China.
Frontiers in Molecular Neuroscience
|June 7, 2023
Summary
Inhibitor of apoptosis, nuclear-localized-associated protein (iASPP) suppresses neuronal development. This study reveals iASPP inhibits neurite outgrowth by dephosphorylating Sptan1, impacting neurodevelopment.
Area of Science:
- Molecular Biology
- Neuroscience
- Cancer Biology
Background:
- Inhibitor of apoptosis, nuclear-localized-associated protein (iASPP) is known to promote cancer cell survival by antagonizing p53's apoptotic activity.
- The function of iASPP in neurodevelopment remains largely uncharacterized.
Purpose of the Study:
- To investigate the role of iASPP in neuronal differentiation and development.
- To elucidate the molecular mechanisms underlying iASPP's regulation of neuronal development.
Main Methods:
- Utilized neuronal differentiation cellular models.
- Employed techniques including immunohistochemistry, RNA interference, gene overexpression, coimmunoprecipitation coupled with mass spectrometry (CoIP-MS), and coimmunoprecipitation (CoIP).
Main Results:
- iASPP expression decreased during neuronal development.
- Silencing iASPP enhanced neuronal differentiation, while its overexpression inhibited neurite differentiation.
- iASPP was found to associate with Sptan1 and dephosphorylate it by recruiting protein phosphatase 1 (PP1).
- Phosphorylation status of Sptbn1 (a related protein) affected neuronal development.
Conclusions:
- iASPP suppresses neurite development by inhibiting Sptan1 phosphorylation.
- This mechanism highlights a novel role for iASPP in regulating neurodevelopment.
Related Concept Videos
01:45Regulation of Nuclear Protein Sorting
2.4K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.4K
01:39Mechanism of Filopodia Formation
2.4K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.4K
01:14Generation of Straight or Branched Actin Filaments
3.0K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
3.0K
01:31Mechanism of Lamellipodia Formation
2.6K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
2.6K
01:45Tail-anchoring of Proteins in the ER Membrane
3.1K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.1K
01:32Assembly of Complex Microtubule Structures
1.9K
Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
1.9K