Malaria Cytoskeletal Proteins Require Alveolin–Alveolin Interactions for Differential Localization
The alveolins are a family of intermediate filament-like proteins that form cytoskeletal structures in both free-living and parasitic members of the alveolate kingdom. Despite their important functions, the alveolins’ biochemical properties and organizing principles are still poorly understood. Here...
Saved in:
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Wiley
2025-01-01
|
| Series: | Cellular Microbiology |
| Online Access: | http://dx.doi.org/10.1155/cmi/4530231 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850117768877178880 |
|---|---|
| author | Ana Karla Cepeda Diaz Peter S. Back Sreelakshmi K. Sreenivasamurthy Jeffrey D. Dvorin |
| author_facet | Ana Karla Cepeda Diaz Peter S. Back Sreelakshmi K. Sreenivasamurthy Jeffrey D. Dvorin |
| author_sort | Ana Karla Cepeda Diaz |
| collection | DOAJ |
| description | The alveolins are a family of intermediate filament-like proteins that form cytoskeletal structures in both free-living and parasitic members of the alveolate kingdom. Despite their important functions, the alveolins’ biochemical properties and organizing principles are still poorly understood. Here, we characterize four alveolins of Plasmodium falciparum, the deadliest malaria parasite, to understand how alveolin domains mediate protein–protein interactions and highly specific recruitment to substructures of the cytoskeleton. Unexpectedly, we uncover variable dependence on alveolin domains for each substructure rather than an overarching mechanism. While PfIMC1e requires 1f to be sequentially recruited to the basal complex, PfIMC1c and PfIMC1g do not require interactions with each other to localize properly to the inner membrane complex. Moreover, alveolin domains are not interchangeable—they contain unique signatures for specialized localization. Finally, we identify a region outside the alveolin domain of PfIMC1e that is important for basal complex recruitment. These results provide direct evidence that alveolin domains mediate both alveolin–alveolin interactions and compartment-specific localization. |
| format | Article |
| id | doaj-art-7e0428163d1747178e73028028dadbd8 |
| institution | OA Journals |
| issn | 1462-5822 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Cellular Microbiology |
| spelling | doaj-art-7e0428163d1747178e73028028dadbd82025-08-20T02:36:02ZengWileyCellular Microbiology1462-58222025-01-01202510.1155/cmi/4530231Malaria Cytoskeletal Proteins Require Alveolin–Alveolin Interactions for Differential LocalizationAna Karla Cepeda Diaz0Peter S. Back1Sreelakshmi K. Sreenivasamurthy2Jeffrey D. Dvorin3Division of Infectious DiseasesDivision of Infectious DiseasesDivision of Infectious DiseasesDivision of Infectious DiseasesThe alveolins are a family of intermediate filament-like proteins that form cytoskeletal structures in both free-living and parasitic members of the alveolate kingdom. Despite their important functions, the alveolins’ biochemical properties and organizing principles are still poorly understood. Here, we characterize four alveolins of Plasmodium falciparum, the deadliest malaria parasite, to understand how alveolin domains mediate protein–protein interactions and highly specific recruitment to substructures of the cytoskeleton. Unexpectedly, we uncover variable dependence on alveolin domains for each substructure rather than an overarching mechanism. While PfIMC1e requires 1f to be sequentially recruited to the basal complex, PfIMC1c and PfIMC1g do not require interactions with each other to localize properly to the inner membrane complex. Moreover, alveolin domains are not interchangeable—they contain unique signatures for specialized localization. Finally, we identify a region outside the alveolin domain of PfIMC1e that is important for basal complex recruitment. These results provide direct evidence that alveolin domains mediate both alveolin–alveolin interactions and compartment-specific localization.http://dx.doi.org/10.1155/cmi/4530231 |
| spellingShingle | Ana Karla Cepeda Diaz Peter S. Back Sreelakshmi K. Sreenivasamurthy Jeffrey D. Dvorin Malaria Cytoskeletal Proteins Require Alveolin–Alveolin Interactions for Differential Localization Cellular Microbiology |
| title | Malaria Cytoskeletal Proteins Require Alveolin–Alveolin Interactions for Differential Localization |
| title_full | Malaria Cytoskeletal Proteins Require Alveolin–Alveolin Interactions for Differential Localization |
| title_fullStr | Malaria Cytoskeletal Proteins Require Alveolin–Alveolin Interactions for Differential Localization |
| title_full_unstemmed | Malaria Cytoskeletal Proteins Require Alveolin–Alveolin Interactions for Differential Localization |
| title_short | Malaria Cytoskeletal Proteins Require Alveolin–Alveolin Interactions for Differential Localization |
| title_sort | malaria cytoskeletal proteins require alveolin alveolin interactions for differential localization |
| url | http://dx.doi.org/10.1155/cmi/4530231 |
| work_keys_str_mv | AT anakarlacepedadiaz malariacytoskeletalproteinsrequirealveolinalveolininteractionsfordifferentiallocalization AT petersback malariacytoskeletalproteinsrequirealveolinalveolininteractionsfordifferentiallocalization AT sreelakshmiksreenivasamurthy malariacytoskeletalproteinsrequirealveolinalveolininteractionsfordifferentiallocalization AT jeffreyddvorin malariacytoskeletalproteinsrequirealveolinalveolininteractionsfordifferentiallocalization |