Activation Mechanisms and Diverse Functions of Mammalian Phospholipase C
Phospholipase C (PLC) plays pivotal roles in regulating various cellular functions by metabolizing phosphatidylinositol 4,5-bisphosphate in the plasma membrane. This process generates two second messengers, inositol 1,4,5-trisphosphate and diacylglycerol, which respectively regulate the intracellula...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-05-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/13/6/915 |
| _version_ | 1797595852559089664 |
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| author | Kaori Kanemaru Yoshikazu Nakamura |
| author_facet | Kaori Kanemaru Yoshikazu Nakamura |
| author_sort | Kaori Kanemaru |
| collection | DOAJ |
| description | Phospholipase C (PLC) plays pivotal roles in regulating various cellular functions by metabolizing phosphatidylinositol 4,5-bisphosphate in the plasma membrane. This process generates two second messengers, inositol 1,4,5-trisphosphate and diacylglycerol, which respectively regulate the intracellular Ca<sup>2+</sup> levels and protein kinase C activation. In mammals, six classes of typical PLC have been identified and classified based on their structure and activation mechanisms. They all share X and Y domains, which are responsible for enzymatic activity, as well as subtype-specific domains. Furthermore, in addition to typical PLC, atypical PLC with unique structures solely harboring an X domain has been recently discovered. Collectively, seven classes and 16 isozymes of mammalian PLC are known to date. Dysregulation of PLC activity has been implicated in several pathophysiological conditions, including cancer, cardiovascular diseases, and neurological disorders. Therefore, identification of new drug targets that can selectively modulate PLC activity is important. The present review focuses on the structures, activation mechanisms, and physiological functions of mammalian PLC. |
| first_indexed | 2024-03-11T02:42:22Z |
| format | Article |
| id | doaj.art-fae8157a06914504b0517f66f8a9f9ab |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-11T02:42:22Z |
| publishDate | 2023-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-fae8157a06914504b0517f66f8a9f9ab2023-11-18T09:30:36ZengMDPI AGBiomolecules2218-273X2023-05-0113691510.3390/biom13060915Activation Mechanisms and Diverse Functions of Mammalian Phospholipase CKaori Kanemaru0Yoshikazu Nakamura1Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Chiba 278-8510, JapanDepartment of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Chiba 278-8510, JapanPhospholipase C (PLC) plays pivotal roles in regulating various cellular functions by metabolizing phosphatidylinositol 4,5-bisphosphate in the plasma membrane. This process generates two second messengers, inositol 1,4,5-trisphosphate and diacylglycerol, which respectively regulate the intracellular Ca<sup>2+</sup> levels and protein kinase C activation. In mammals, six classes of typical PLC have been identified and classified based on their structure and activation mechanisms. They all share X and Y domains, which are responsible for enzymatic activity, as well as subtype-specific domains. Furthermore, in addition to typical PLC, atypical PLC with unique structures solely harboring an X domain has been recently discovered. Collectively, seven classes and 16 isozymes of mammalian PLC are known to date. Dysregulation of PLC activity has been implicated in several pathophysiological conditions, including cancer, cardiovascular diseases, and neurological disorders. Therefore, identification of new drug targets that can selectively modulate PLC activity is important. The present review focuses on the structures, activation mechanisms, and physiological functions of mammalian PLC.https://www.mdpi.com/2218-273X/13/6/915phospholipase Cphosphatidylinositol 4,5-bisphosphateinositol 1,4,5-trisphosphatediacylglycerol |
| spellingShingle | Kaori Kanemaru Yoshikazu Nakamura Activation Mechanisms and Diverse Functions of Mammalian Phospholipase C Biomolecules phospholipase C phosphatidylinositol 4,5-bisphosphate inositol 1,4,5-trisphosphate diacylglycerol |
| title | Activation Mechanisms and Diverse Functions of Mammalian Phospholipase C |
| title_full | Activation Mechanisms and Diverse Functions of Mammalian Phospholipase C |
| title_fullStr | Activation Mechanisms and Diverse Functions of Mammalian Phospholipase C |
| title_full_unstemmed | Activation Mechanisms and Diverse Functions of Mammalian Phospholipase C |
| title_short | Activation Mechanisms and Diverse Functions of Mammalian Phospholipase C |
| title_sort | activation mechanisms and diverse functions of mammalian phospholipase c |
| topic | phospholipase C phosphatidylinositol 4,5-bisphosphate inositol 1,4,5-trisphosphate diacylglycerol |
| url | https://www.mdpi.com/2218-273X/13/6/915 |
| work_keys_str_mv | AT kaorikanemaru activationmechanismsanddiversefunctionsofmammalianphospholipasec AT yoshikazunakamura activationmechanismsanddiversefunctionsofmammalianphospholipasec |