The Biochemical Properties and Functions of CALM and AP180 in Clathrin Mediated Endocytosis
Clathrin-mediated endocytosis (CME) is a fundamental process for the regulated internalization of transmembrane cargo and ligands via the formation of vesicles using a clathrin coat. A vesicle coat is initially created at the plasma membrane by clathrin assembly into a lattice, while a specific carg...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2014-07-01
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| Series: | Membranes |
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| Online Access: | http://www.mdpi.com/2077-0375/4/3/388 |
| _version_ | 1797725347945381888 |
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| author | Lia Moshkanbaryans Ling-Shan Chan Mark E. Graham |
| author_facet | Lia Moshkanbaryans Ling-Shan Chan Mark E. Graham |
| author_sort | Lia Moshkanbaryans |
| collection | DOAJ |
| description | Clathrin-mediated endocytosis (CME) is a fundamental process for the regulated internalization of transmembrane cargo and ligands via the formation of vesicles using a clathrin coat. A vesicle coat is initially created at the plasma membrane by clathrin assembly into a lattice, while a specific cargo sorting process selects and concentrates proteins for inclusion in the new vesicle. Vesicles formed via CME traffic to different parts of the cell and fuse with target membranes to deliver cargo. Both clathrin assembly and cargo sorting functions are features of the two gene family consisting of assembly protein 180 kDa (AP180) and clathrin assembly lymphoid myeloid leukemia protein (CALM). In this review, we compare the primary structure and domain organization of CALM and AP180 and relate these properties to known functions and roles in CME and disease. |
| first_indexed | 2024-03-12T10:29:53Z |
| format | Article |
| id | doaj.art-939c1bf99fe24c0e9ef48f3aa86afdec |
| institution | Directory Open Access Journal |
| issn | 2077-0375 |
| language | English |
| last_indexed | 2024-03-12T10:29:53Z |
| publishDate | 2014-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Membranes |
| spelling | doaj.art-939c1bf99fe24c0e9ef48f3aa86afdec2023-09-02T09:20:07ZengMDPI AGMembranes2077-03752014-07-014338841310.3390/membranes4030388membranes4030388The Biochemical Properties and Functions of CALM and AP180 in Clathrin Mediated EndocytosisLia Moshkanbaryans0Ling-Shan Chan1Mark E. Graham2Children's Medical Research Institute, The University of Sydney, 214 Hawkesbury Road, Westmead, NSW 2145, AustraliaChildren's Medical Research Institute, The University of Sydney, 214 Hawkesbury Road, Westmead, NSW 2145, AustraliaChildren's Medical Research Institute, The University of Sydney, 214 Hawkesbury Road, Westmead, NSW 2145, AustraliaClathrin-mediated endocytosis (CME) is a fundamental process for the regulated internalization of transmembrane cargo and ligands via the formation of vesicles using a clathrin coat. A vesicle coat is initially created at the plasma membrane by clathrin assembly into a lattice, while a specific cargo sorting process selects and concentrates proteins for inclusion in the new vesicle. Vesicles formed via CME traffic to different parts of the cell and fuse with target membranes to deliver cargo. Both clathrin assembly and cargo sorting functions are features of the two gene family consisting of assembly protein 180 kDa (AP180) and clathrin assembly lymphoid myeloid leukemia protein (CALM). In this review, we compare the primary structure and domain organization of CALM and AP180 and relate these properties to known functions and roles in CME and disease.http://www.mdpi.com/2077-0375/4/3/388CALMphosphatidylinositol binding clathrin assembly proteinAP180clathrinadapter protein complex 2endocytosisvesicleclathrin assemblycargo sortingAP180 N-terminal homology domainphosphorylationO-GlcNAc-6-phosphate |
| spellingShingle | Lia Moshkanbaryans Ling-Shan Chan Mark E. Graham The Biochemical Properties and Functions of CALM and AP180 in Clathrin Mediated Endocytosis Membranes CALM phosphatidylinositol binding clathrin assembly protein AP180 clathrin adapter protein complex 2 endocytosis vesicle clathrin assembly cargo sorting AP180 N-terminal homology domain phosphorylation O-GlcNAc-6-phosphate |
| title | The Biochemical Properties and Functions of CALM and AP180 in Clathrin Mediated Endocytosis |
| title_full | The Biochemical Properties and Functions of CALM and AP180 in Clathrin Mediated Endocytosis |
| title_fullStr | The Biochemical Properties and Functions of CALM and AP180 in Clathrin Mediated Endocytosis |
| title_full_unstemmed | The Biochemical Properties and Functions of CALM and AP180 in Clathrin Mediated Endocytosis |
| title_short | The Biochemical Properties and Functions of CALM and AP180 in Clathrin Mediated Endocytosis |
| title_sort | biochemical properties and functions of calm and ap180 in clathrin mediated endocytosis |
| topic | CALM phosphatidylinositol binding clathrin assembly protein AP180 clathrin adapter protein complex 2 endocytosis vesicle clathrin assembly cargo sorting AP180 N-terminal homology domain phosphorylation O-GlcNAc-6-phosphate |
| url | http://www.mdpi.com/2077-0375/4/3/388 |
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