25.10
Introducción a la actina
La actina es una proteína citoesquelética altamente conservada que se encuentra en abundancia en las células eucariotas. Constituye el 10 % del peso d…
En el citoesqueleto, las actinas son los componentes básicos de los microfilamentos del citoesqueleto. Los monómeros de actina tienen una forma redonda y se denominan globulares o G-actina.
Estos monómeros se polimerizan de la cabeza a la cola formando una estructura helicoidal apretada y dextrógira llamada filamentosa o F-actina.
Cada subunidad de actina tiene un dominio externo e interno unidos por una hélice enlazadora más pequeña. Tal disposición forma dos hendiduras: la hendidura superior se une a un ion ATP y un ion de magnesio. La hendidura hidrofóbica inferior es específica para las proteínas de unión a actina.
La G-actina tiene una baja actividad de ATPasa que se ve reforzada en la F-actina. Cuando un complejo ATP-G-actina se une a la F-actina, el ATP se hidroliza a ADP y fosfato, formando un filamento altamente estable.
El extremo creciente de la F-actina unido a ATP se denomina extremo positivo, mientras que el otro extremo, unido a ADP, es el extremo negativo.
Las actinas tienen diferentes isoformas, ampliamente clasificadas en alfa, beta y gamma. Se expresan en diferentes tipos de células, como la α-actina en las fibras musculares contráctiles, la β-actina en la corteza celular y la γ-actina en las fibras musculares lisas.
View the full transcript and gain access to JoVE Core videos
Q1: What is the difference between G-actin and F-actin?
G-actin (globular actin) refers to individual actin monomers with a round shape, while F-actin (filamentous actin) forms when G-actin monomers polymerize head-to-tail into a tight, right-handed helical structure. F-actin has enhanced ATPase activity compared to the low activity of G-actin, and this structural transformation is fundamental to actin polymerization.
Q2: How does ATP binding affect actin filament stability?
When ATP-bound G-actin binds to F-actin, the ATP is hydrolyzed to ADP and phosphate, forming a highly stable filament. The ATP-bound growing end is called the plus-end, while the ADP-bound end is the minus-end. This ATP hydrolysis is critical for maintaining filament stability and polarity.
Q3: What structural features allow actin to bind other proteins?
Each actin subunit contains an outer and inner domain connected by a linker helix, creating two clefts. The upper cleft binds ATP and magnesium ions, while the lower hydrophobic cleft is specific for actin-binding proteins. This arrangement enables actin to interact with diverse regulatory and structural proteins.
Q4: What are the three main classes of actin isoforms and where are they expressed?
Actin isoforms are classified into alpha, beta, and gamma types based on their isoelectric points. Alpha-actin is expressed in contractile muscle fibers, beta-actin in the cell cortex, and gamma-actin in smooth muscle fibers. These tissue-specific isoforms are nearly identical but have distinct cellular roles.
Q5: Why is actin considered a highly conserved protein across species?
Actin found in unicellular amoebae and complex multicellular animals is approximately 80% similar, demonstrating conservation over a billion years of evolution. Additionally, actins in yeast and humans share 87% similarity. This conservation reflects actin's fundamental importance in cellular functions across diverse organisms.
Q6: What percentage of total cellular protein does actin represent in different cell types?
In muscle cells, actin constitutes approximately 10% of total cellular protein by weight, making it exceptionally abundant. In non-muscle cells, actin comprises only 1-5% of total cellular protein. This difference reflects the distinct metabolic demands and structural requirements of contractile versus non-contractile cells.
Q7: How do actin filaments contribute to cellular processes beyond muscle contraction?
Beyond muscle contraction, actin filaments play essential roles in cell migration, cell adhesion, cell division, protein trafficking, and membrane organization. The discovery of actin in non-muscle cells during the early 1970s revealed its broad importance in the role of actin and myosin in non-muscle cells.